Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7389, pp. 336 - 340
Cells are organized on length scales ranging from angstrom to micrometres. However, the mechanisms by which angstrom-scale molecular properties are translated...
POLYMERS | MOTIFS | NUCLEAR-BODIES | RNA | MULTIDISCIPLINARY SCIENCES | NCK | MECHANISMS | POLYMERIZATION | TRANSLATION | GRANULES | DOMAINS | Adaptor Proteins, Signal Transducing - chemistry | Biopolymers - chemistry | Phosphorylation | Fluorescence Recovery After Photobleaching | Humans | Wiskott-Aldrich Syndrome Protein, Neuronal - chemistry | Biopolymers - metabolism | Phase Transition | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Protein Structure, Quaternary | Membrane Proteins - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | Binding Sites | Oncogene Proteins - chemistry | Signal Transduction | Oncogene Proteins - metabolism | src Homology Domains | Proline-Rich Protein Domains | Multiprotein Complexes - chemistry | Proteins - metabolism | Membrane Proteins - chemistry | Ligands | HeLa Cells | Proteins - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Wiskott-Aldrich syndrome | Protein research | Macromolecules | Physiological aspects | Phase transformations (Statistical physics) | Research | Properties | Phosphotransferases | Proteins | Experiments | Physical properties | Binding sites
POLYMERS | MOTIFS | NUCLEAR-BODIES | RNA | MULTIDISCIPLINARY SCIENCES | NCK | MECHANISMS | POLYMERIZATION | TRANSLATION | GRANULES | DOMAINS | Adaptor Proteins, Signal Transducing - chemistry | Biopolymers - chemistry | Phosphorylation | Fluorescence Recovery After Photobleaching | Humans | Wiskott-Aldrich Syndrome Protein, Neuronal - chemistry | Biopolymers - metabolism | Phase Transition | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Protein Structure, Quaternary | Membrane Proteins - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | Binding Sites | Oncogene Proteins - chemistry | Signal Transduction | Oncogene Proteins - metabolism | src Homology Domains | Proline-Rich Protein Domains | Multiprotein Complexes - chemistry | Proteins - metabolism | Membrane Proteins - chemistry | Ligands | HeLa Cells | Proteins - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Wiskott-Aldrich syndrome | Protein research | Macromolecules | Physiological aspects | Phase transformations (Statistical physics) | Research | Properties | Phosphotransferases | Proteins | Experiments | Physical properties | Binding sites
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 06/2016, Volume 41, Issue 6, pp. 478 - 490
Two types of sequences, proline-rich domains (PRDs) and the WASP-homology 2 (WH2) domain, are found in most actin filament nucleation and elongation factors...
PROMOTING FACTOR | ATP-ACTIN | CORDON-BLEU | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RICKETTSIA SCA2 | ARP2/3 COMPLEX | SYNDAPIN I | MUSCLE-CELLS | BACTERIAL EFFECTOR VOPL | FILAMENT NUCLEATION | Autoantigens - metabolism | Cytoskeletal Proteins - genetics | Actin-Related Protein 2-3 Complex - ultrastructure | Humans | Actins - metabolism | Fetal Proteins - metabolism | Autoantigens - genetics | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cell Nucleus - metabolism | Actins - chemistry | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Amino Acid Sequence | Microfilament Proteins - chemistry | Bacteria - metabolism | Actin Cytoskeleton - metabolism | Protein Structure, Secondary | Polymerization | Nuclear Proteins - metabolism | Autoantigens - chemistry | Cytoskeletal Proteins - chemistry | Nuclear Proteins - chemistry | Bacteria - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Cell Nucleus - genetics | Fetal Proteins - genetics | Actin Cytoskeleton - ultrastructure | Fetal Proteins - chemistry | Physiological aspects | Muscle proteins | Actin | Protein-protein interactions | Protein binding
PROMOTING FACTOR | ATP-ACTIN | CORDON-BLEU | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RICKETTSIA SCA2 | ARP2/3 COMPLEX | SYNDAPIN I | MUSCLE-CELLS | BACTERIAL EFFECTOR VOPL | FILAMENT NUCLEATION | Autoantigens - metabolism | Cytoskeletal Proteins - genetics | Actin-Related Protein 2-3 Complex - ultrastructure | Humans | Actins - metabolism | Fetal Proteins - metabolism | Autoantigens - genetics | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cell Nucleus - metabolism | Actins - chemistry | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Amino Acid Sequence | Microfilament Proteins - chemistry | Bacteria - metabolism | Actin Cytoskeleton - metabolism | Protein Structure, Secondary | Polymerization | Nuclear Proteins - metabolism | Autoantigens - chemistry | Cytoskeletal Proteins - chemistry | Nuclear Proteins - chemistry | Bacteria - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Cell Nucleus - genetics | Fetal Proteins - genetics | Actin Cytoskeleton - ultrastructure | Fetal Proteins - chemistry | Physiological aspects | Muscle proteins | Actin | Protein-protein interactions | Protein binding
Journal Article
Cancer Medicine, ISSN 2045-7634, 07/2017, Volume 6, Issue 7, pp. 1707 - 1719
Current staging is inadequate for predicting clinical outcome of esophageal squamous cell carcinoma (ESCC). Aberrant expression of LOXL2 and actin‐related...
lysyl oxidase‐like 2 | esophageal squamous cell carcinoma | three‐gene signature | prognosis | protein–protein interaction network | Actin‐related proteins | lysyl oxidase-like 2 | three-gene signature | Actin-related proteins | LYSYL OXIDASE | protein-protein interaction network | E-CADHERIN | FIBRONECTIN 1 | LYMPH-NODE METASTASIS | ONCOLOGY | ARCHITECTURE | LEADS | OXIDASE-LIKE 2 | EXPRESSION | PROGRESSION | Prognosis | Carcinoma, Squamous Cell - genetics | Carcinoma, Squamous Cell - metabolism | Carcinoma, Squamous Cell - pathology | Humans | Actins - metabolism | Gene Expression Regulation, Neoplastic | Male | Gene Expression Profiling | Amino Acid Oxidoreductases - metabolism | Biomarkers, Tumor | Esophageal Neoplasms - pathology | Protein Interaction Maps | Amino Acid Oxidoreductases - genetics | Carcinoma, Squamous Cell - mortality | Esophageal Neoplasms - metabolism | Esophageal Neoplasms - mortality | Female | Esophageal Squamous Cell Carcinoma | Cell Line | Computational Biology - methods | Reproducibility of Results | Kaplan-Meier Estimate | Protein Interaction Mapping | Esophageal Neoplasms - genetics | Cytoskeleton | ROC Curve | Neoplasm Staging | Oxidases | Fibronectins | Squamous cell carcinoma | RNA | Actin | Genes | Genomics | Genetic research | Muscle proteins | Protein-protein interactions | Esophageal cancer
lysyl oxidase‐like 2 | esophageal squamous cell carcinoma | three‐gene signature | prognosis | protein–protein interaction network | Actin‐related proteins | lysyl oxidase-like 2 | three-gene signature | Actin-related proteins | LYSYL OXIDASE | protein-protein interaction network | E-CADHERIN | FIBRONECTIN 1 | LYMPH-NODE METASTASIS | ONCOLOGY | ARCHITECTURE | LEADS | OXIDASE-LIKE 2 | EXPRESSION | PROGRESSION | Prognosis | Carcinoma, Squamous Cell - genetics | Carcinoma, Squamous Cell - metabolism | Carcinoma, Squamous Cell - pathology | Humans | Actins - metabolism | Gene Expression Regulation, Neoplastic | Male | Gene Expression Profiling | Amino Acid Oxidoreductases - metabolism | Biomarkers, Tumor | Esophageal Neoplasms - pathology | Protein Interaction Maps | Amino Acid Oxidoreductases - genetics | Carcinoma, Squamous Cell - mortality | Esophageal Neoplasms - metabolism | Esophageal Neoplasms - mortality | Female | Esophageal Squamous Cell Carcinoma | Cell Line | Computational Biology - methods | Reproducibility of Results | Kaplan-Meier Estimate | Protein Interaction Mapping | Esophageal Neoplasms - genetics | Cytoskeleton | ROC Curve | Neoplasm Staging | Oxidases | Fibronectins | Squamous cell carcinoma | RNA | Actin | Genes | Genomics | Genetic research | Muscle proteins | Protein-protein interactions | Esophageal cancer
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 1/2005, Volume 168, Issue 3, pp. 441 - 452
Invadopodia are actin-rich membrane protrusions with a matrix degradation activity formed by invasive cancer cells. We have studied the molecular mechanisms of...
Receptors | Microfilaments | Actin depolymerizing factors | Small interfering RNA | Actins | Antibodies | Polymerization | Cultured cells | Cell membranes | Cells | CARCINOMA-CELLS | GROWTH-FACTOR RECEPTOR | MAMMARY ADENOCARCINOMA | ACTIN POLYMERIZATION | LAMELLIPOD EXTENSION | N-WASP | EXTRACELLULAR-MATRIX | SPECIALIZED SURFACE PROTRUSIONS | ALDRICH-SYNDROME PROTEIN | INVASIVE CELLS | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Epidermal Growth Factor - physiology | Cytoskeletal Proteins - genetics | Actins - metabolism | Microfilament Proteins - physiology | Extracellular Matrix - metabolism | cdc42 GTP-Binding Protein - metabolism | Quinazolines | Oncogene Proteins - physiology | Cell Movement - physiology | Transfection | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Cytoskeletal Proteins - physiology | Wiskott-Aldrich Syndrome Protein Family | Microfilament Proteins - genetics | Carrier Proteins - physiology | Nerve Tissue Proteins - physiology | Wiskott-Aldrich Syndrome Protein, Neuronal | Cell Surface Extensions - metabolism | Neoplasm Invasiveness | RNA, Small Interfering - pharmacology | Enzyme Inhibitors - pharmacology | Oncogene Proteins - metabolism | Rats | Tyrphostins - pharmacology | Actin Depolymerizing Factors | cdc42 GTP-Binding Protein - physiology | Nerve Tissue Proteins - genetics | Fibronectins - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing - physiology | Animals | Carrier Proteins - metabolism | GRB2 Adaptor Protein | Models, Biological | cdc42 GTP-Binding Protein - genetics | Cell Surface Extensions - drug effects | Adaptor Proteins, Signal Transducing - genetics | Actin-Related Protein 2 | Cell Line, Tumor | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Actin-Related Protein 3 | Adaptor Proteins, Signal Transducing - metabolism | Microscopy, Fluorescence | Cell Surface Extensions - physiology | Epidermal growth factor | Metastasis | Cancer invasiveness | Cancer cells
Receptors | Microfilaments | Actin depolymerizing factors | Small interfering RNA | Actins | Antibodies | Polymerization | Cultured cells | Cell membranes | Cells | CARCINOMA-CELLS | GROWTH-FACTOR RECEPTOR | MAMMARY ADENOCARCINOMA | ACTIN POLYMERIZATION | LAMELLIPOD EXTENSION | N-WASP | EXTRACELLULAR-MATRIX | SPECIALIZED SURFACE PROTRUSIONS | ALDRICH-SYNDROME PROTEIN | INVASIVE CELLS | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Epidermal Growth Factor - physiology | Cytoskeletal Proteins - genetics | Actins - metabolism | Microfilament Proteins - physiology | Extracellular Matrix - metabolism | cdc42 GTP-Binding Protein - metabolism | Quinazolines | Oncogene Proteins - physiology | Cell Movement - physiology | Transfection | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Cytoskeletal Proteins - physiology | Wiskott-Aldrich Syndrome Protein Family | Microfilament Proteins - genetics | Carrier Proteins - physiology | Nerve Tissue Proteins - physiology | Wiskott-Aldrich Syndrome Protein, Neuronal | Cell Surface Extensions - metabolism | Neoplasm Invasiveness | RNA, Small Interfering - pharmacology | Enzyme Inhibitors - pharmacology | Oncogene Proteins - metabolism | Rats | Tyrphostins - pharmacology | Actin Depolymerizing Factors | cdc42 GTP-Binding Protein - physiology | Nerve Tissue Proteins - genetics | Fibronectins - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing - physiology | Animals | Carrier Proteins - metabolism | GRB2 Adaptor Protein | Models, Biological | cdc42 GTP-Binding Protein - genetics | Cell Surface Extensions - drug effects | Adaptor Proteins, Signal Transducing - genetics | Actin-Related Protein 2 | Cell Line, Tumor | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Actin-Related Protein 3 | Adaptor Proteins, Signal Transducing - metabolism | Microscopy, Fluorescence | Cell Surface Extensions - physiology | Epidermal growth factor | Metastasis | Cancer invasiveness | Cancer cells
Journal Article
The EMBO Journal, ISSN 0261-4189, 06/2011, Volume 30, Issue 11, pp. 2153 - 2166
Nuclear actin and actin‐related proteins (Arps) are integral components of various chromatin‐remodelling complexes. Actin in such nuclear assemblies does not...
INO80 complex | structural biology | chromatin‐remodelling | actin‐related proteins | nuclear actin | chromatin-remodelling | actin-related proteins | SYSTEM | ALPHA-ACTIN | X-RAY SOLUTION | CHROMATIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | ARP2/3 COMPLEX | INO80 | CELL BIOLOGY | LATRUNCULIN | BINDING | SCATTERING | Protein Structure, Tertiary | Amino Acid Sequence | Microfilament Proteins - chemistry | Saccharomyces cerevisiae - physiology | Protein Multimerization | Actins - metabolism | Models, Molecular | Molecular Sequence Data | Scattering, Small Angle | Crystallography, X-Ray | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Actins - chemistry | Protein Binding | Microfilament Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Polymerization | Chromatin | Biochemistry | Molecular biology | Crystal structure
INO80 complex | structural biology | chromatin‐remodelling | actin‐related proteins | nuclear actin | chromatin-remodelling | actin-related proteins | SYSTEM | ALPHA-ACTIN | X-RAY SOLUTION | CHROMATIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | ARP2/3 COMPLEX | INO80 | CELL BIOLOGY | LATRUNCULIN | BINDING | SCATTERING | Protein Structure, Tertiary | Amino Acid Sequence | Microfilament Proteins - chemistry | Saccharomyces cerevisiae - physiology | Protein Multimerization | Actins - metabolism | Models, Molecular | Molecular Sequence Data | Scattering, Small Angle | Crystallography, X-Ray | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Actins - chemistry | Protein Binding | Microfilament Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Polymerization | Chromatin | Biochemistry | Molecular biology | Crystal structure
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 9/2003, Volume 162, Issue 6, pp. 1079 - 1088
Cell migration occurs through the protrusion of the actin-enriched lamella. Here, we investigated the effects of RNAi depletion of ∼90 proteins implicated in...
Cell motility | Scars | Delta cells | Microfilaments | Neurons | Drosophila | Cell lines | Actins | Actin depolymerizing factors | Cells | Polymerization | Lamella | Cytokinesis | Actin | SCAR | RNA INTERFERENCE | MIGRATION | polymerization | lamella | cytokinesis | ARP2/3 COMPLEX | HOMOLOG | MOTILITY DRIVEN | CELL BIOLOGY | YEAST | actin | FILAMENTS | CYCLASE-ASSOCIATED PROTEIN | DYNAMICS | NUCLEATION | Pseudopodia - ultrastructure | Cytoskeletal Proteins - antagonists & inhibitors | Cytoskeletal Proteins - genetics | Actins - metabolism | rac GTP-Binding Proteins - metabolism | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Cell Movement - physiology | Actins - genetics | Cell Cycle Proteins - antagonists & inhibitors | Actins - deficiency | RNA Interference | Profilins | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Destrin | Drosophila Proteins - antagonists & inhibitors | Microfilament Proteins - genetics | Cell Line | Actin Cytoskeleton - metabolism | Microfilament Proteins - deficiency | Carrier Proteins - antagonists & inhibitors | Cell Cycle Proteins - metabolism | Actin Depolymerizing Factors | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing | Actins - antagonists & inhibitors | Animals | Carrier Proteins - metabolism | Microfilament Proteins - antagonists & inhibitors | Caenorhabditis elegans Proteins - antagonists & inhibitors | Pseudopodia - metabolism | Drosophila Proteins - deficiency | Actin-Related Protein 2 | Eukaryotic Cells - cytology | Drosophila Proteins - genetics | Actin Cytoskeleton - ultrastructure | Caenorhabditis elegans Proteins - genetics | Drosophila melanogaster | Contractile Proteins | RNA | Listeria | Bacterial proteins | Cytology | Physiological aspects | Genetic aspects | Research | Cell migration | actin; lamella; polymerization; SCAR; cytokinesis
Cell motility | Scars | Delta cells | Microfilaments | Neurons | Drosophila | Cell lines | Actins | Actin depolymerizing factors | Cells | Polymerization | Lamella | Cytokinesis | Actin | SCAR | RNA INTERFERENCE | MIGRATION | polymerization | lamella | cytokinesis | ARP2/3 COMPLEX | HOMOLOG | MOTILITY DRIVEN | CELL BIOLOGY | YEAST | actin | FILAMENTS | CYCLASE-ASSOCIATED PROTEIN | DYNAMICS | NUCLEATION | Pseudopodia - ultrastructure | Cytoskeletal Proteins - antagonists & inhibitors | Cytoskeletal Proteins - genetics | Actins - metabolism | rac GTP-Binding Proteins - metabolism | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Cell Movement - physiology | Actins - genetics | Cell Cycle Proteins - antagonists & inhibitors | Actins - deficiency | RNA Interference | Profilins | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Destrin | Drosophila Proteins - antagonists & inhibitors | Microfilament Proteins - genetics | Cell Line | Actin Cytoskeleton - metabolism | Microfilament Proteins - deficiency | Carrier Proteins - antagonists & inhibitors | Cell Cycle Proteins - metabolism | Actin Depolymerizing Factors | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing | Actins - antagonists & inhibitors | Animals | Carrier Proteins - metabolism | Microfilament Proteins - antagonists & inhibitors | Caenorhabditis elegans Proteins - antagonists & inhibitors | Pseudopodia - metabolism | Drosophila Proteins - deficiency | Actin-Related Protein 2 | Eukaryotic Cells - cytology | Drosophila Proteins - genetics | Actin Cytoskeleton - ultrastructure | Caenorhabditis elegans Proteins - genetics | Drosophila melanogaster | Contractile Proteins | RNA | Listeria | Bacterial proteins | Cytology | Physiological aspects | Genetic aspects | Research | Cell migration | actin; lamella; polymerization; SCAR; cytokinesis
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 8/2009, Volume 186, Issue 4, pp. 571 - 587
Invadopodia are matrix-degrading membrane protrusions in invasive carcinoma cells. The mechanisms regulating invadopodium assembly and maturation are not...
Phosphorylation | Quantification | Cell lines | Actin depolymerizing factors | Actins | Polymerization | Small interfering RNA | Antibodies | Protein precursors | Physiological regulation | CARCINOMA-CELLS | TYROSINE PHOSPHORYLATION | EGF | PATHWAY | ACTIN POLYMERIZATION | IN-VIVO | CANCER-CELL INVASION | EXTRACELLULAR-MATRIX DEGRADATION | ARP2/3 COMPLEX | PODOSOME FORMATION | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Oncogene Protein pp60(v-src) - metabolism | Actin Depolymerizing Factors - genetics | Humans | Actins - metabolism | Extracellular Matrix - metabolism | Actin-Related Protein 2-3 Complex - genetics | Recombinant Fusion Proteins - metabolism | Actin Depolymerizing Factors - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | Protein Structure, Tertiary | Neoplasm Invasiveness | Oncogene Proteins - metabolism | Rats | Epidermal Growth Factor - metabolism | Oncogene Protein pp60(v-src) - genetics | Cortactin - metabolism | Matrix Metalloproteinase 14 - metabolism | Mammary Neoplasms, Animal - pathology | Tyrosine - metabolism | Animals | Cortactin - genetics | Mammary Neoplasms, Animal - metabolism | Adaptor Proteins, Signal Transducing - genetics | Matrix Metalloproteinase 14 - genetics | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - genetics | RNA, Small Interfering - metabolism | Metastasis | Properties | Observations | Actin | Cancer cells | Membrane proteins
Phosphorylation | Quantification | Cell lines | Actin depolymerizing factors | Actins | Polymerization | Small interfering RNA | Antibodies | Protein precursors | Physiological regulation | CARCINOMA-CELLS | TYROSINE PHOSPHORYLATION | EGF | PATHWAY | ACTIN POLYMERIZATION | IN-VIVO | CANCER-CELL INVASION | EXTRACELLULAR-MATRIX DEGRADATION | ARP2/3 COMPLEX | PODOSOME FORMATION | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Oncogene Protein pp60(v-src) - metabolism | Actin Depolymerizing Factors - genetics | Humans | Actins - metabolism | Extracellular Matrix - metabolism | Actin-Related Protein 2-3 Complex - genetics | Recombinant Fusion Proteins - metabolism | Actin Depolymerizing Factors - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | Protein Structure, Tertiary | Neoplasm Invasiveness | Oncogene Proteins - metabolism | Rats | Epidermal Growth Factor - metabolism | Oncogene Protein pp60(v-src) - genetics | Cortactin - metabolism | Matrix Metalloproteinase 14 - metabolism | Mammary Neoplasms, Animal - pathology | Tyrosine - metabolism | Animals | Cortactin - genetics | Mammary Neoplasms, Animal - metabolism | Adaptor Proteins, Signal Transducing - genetics | Matrix Metalloproteinase 14 - genetics | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal - genetics | RNA, Small Interfering - metabolism | Metastasis | Properties | Observations | Actin | Cancer cells | Membrane proteins
Journal Article
Cell, ISSN 0092-8674, 04/1999, Volume 97, Issue 2, pp. 221 - 231
Although small GTP-binding proteins of the Rho family have been implicated in signaling to the actin cytoskeleton, the exact nature of the linkage has remained...
LISTERIA-MONOCYTOGENES | CYTOSKELETON | RAC | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHO | REORGANIZATION | DEPOLYMERIZING PROTEIN | ALDRICH-SYNDROME PROTEIN | BINDING | MOTILITY | CELL BIOLOGY | Cytoskeletal Proteins | Xenopus | Actins - metabolism | Biopolymers - metabolism | Phosphatidylinositol 4,5-Diphosphate - metabolism | Nerve Tissue Proteins - chemistry | Cattle | Female | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal | Signal Transduction | Oocytes - metabolism | Cell Cycle Proteins - metabolism | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Nerve Tissue Proteins - genetics | Macromolecular Substances | Nerve Tissue Proteins - metabolism | Peptide Fragments - chemistry | Animals | Models, Biological | Actin-Related Protein 2 | Actin-Related Protein 3 | cdc42 GTP-Binding Protein | In Vitro Techniques | GTP-Binding Proteins - metabolism | Actin | Polymerization | Cellular signal transduction | Muscle proteins | Binding proteins | Cells | Protein binding | Proteins | Cytoskeleton | Research
LISTERIA-MONOCYTOGENES | CYTOSKELETON | RAC | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHO | REORGANIZATION | DEPOLYMERIZING PROTEIN | ALDRICH-SYNDROME PROTEIN | BINDING | MOTILITY | CELL BIOLOGY | Cytoskeletal Proteins | Xenopus | Actins - metabolism | Biopolymers - metabolism | Phosphatidylinositol 4,5-Diphosphate - metabolism | Nerve Tissue Proteins - chemistry | Cattle | Female | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Wiskott-Aldrich Syndrome Protein, Neuronal | Signal Transduction | Oocytes - metabolism | Cell Cycle Proteins - metabolism | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Nerve Tissue Proteins - genetics | Macromolecular Substances | Nerve Tissue Proteins - metabolism | Peptide Fragments - chemistry | Animals | Models, Biological | Actin-Related Protein 2 | Actin-Related Protein 3 | cdc42 GTP-Binding Protein | In Vitro Techniques | GTP-Binding Proteins - metabolism | Actin | Polymerization | Cellular signal transduction | Muscle proteins | Binding proteins | Cells | Protein binding | Proteins | Cytoskeleton | Research
Journal Article
Molecular Biology of the Cell, ISSN 1059-1524, 08/2010, Volume 21, Issue 16, pp. 2880 - 2893
WASP family proteins control actin polymerization by activating the Arp2/3 complex. Several subfamilies exist, but their regulation and physiological roles are...
ACTIVATION | DOMAIN | WASP/SCAR PROTEINS | MECHANISM | STRUCTURAL BASIS | ARP2/3 COMPLEX | N-WASP | ALDRICH-SYNDROME PROTEIN | BINDING | ACTIN NUCLEATION FACTOR | CELL BIOLOGY | Wiskott-Aldrich Syndrome Protein - genetics | Wiskott-Aldrich Syndrome Protein Family - classification | Humans | Molecular Sequence Data | Actin-Related Protein 2-3 Complex - genetics | Green Fluorescent Proteins - genetics | Phylogeny | Protozoan Proteins - genetics | Wiskott-Aldrich Syndrome Protein - classification | Actin-Related Protein 2-3 Complex - metabolism | Protozoan Proteins - metabolism | Conserved Sequence | Wiskott-Aldrich Syndrome Protein - metabolism | Dictyostelium - cytology | Wiskott-Aldrich Syndrome Protein Family - genetics | Amino Acid Sequence | Wiskott-Aldrich Syndrome Protein Family - metabolism | Green Fluorescent Proteins - classification | Binding Sites - genetics | Protozoan Proteins - physiology | Amino Acid Motifs | Sequence Homology, Amino Acid | Animals | Green Fluorescent Proteins - physiology | Microscopy, Fluorescence - methods | Dictyostelium - genetics | Dictyostelium - metabolism | Evolution, Molecular
ACTIVATION | DOMAIN | WASP/SCAR PROTEINS | MECHANISM | STRUCTURAL BASIS | ARP2/3 COMPLEX | N-WASP | ALDRICH-SYNDROME PROTEIN | BINDING | ACTIN NUCLEATION FACTOR | CELL BIOLOGY | Wiskott-Aldrich Syndrome Protein - genetics | Wiskott-Aldrich Syndrome Protein Family - classification | Humans | Molecular Sequence Data | Actin-Related Protein 2-3 Complex - genetics | Green Fluorescent Proteins - genetics | Phylogeny | Protozoan Proteins - genetics | Wiskott-Aldrich Syndrome Protein - classification | Actin-Related Protein 2-3 Complex - metabolism | Protozoan Proteins - metabolism | Conserved Sequence | Wiskott-Aldrich Syndrome Protein - metabolism | Dictyostelium - cytology | Wiskott-Aldrich Syndrome Protein Family - genetics | Amino Acid Sequence | Wiskott-Aldrich Syndrome Protein Family - metabolism | Green Fluorescent Proteins - classification | Binding Sites - genetics | Protozoan Proteins - physiology | Amino Acid Motifs | Sequence Homology, Amino Acid | Animals | Green Fluorescent Proteins - physiology | Microscopy, Fluorescence - methods | Dictyostelium - genetics | Dictyostelium - metabolism | Evolution, Molecular
Journal Article
Biochemical Journal, ISSN 0264-6021, 08/2004, Volume 382, Issue 1, pp. 13 - 25
Cortactin was first identified over a decade ago, and its initial characterization as both an F-actin binding protein and v-Src substrate suggested that it was...
Actin-related protein (Arp2/3) complex | Cell motility | Endocytosis | Suppressor of cAMP receptor (SCAR)/WASP family verprolin homologous (WAVE) | Wiskott-Aldrich syndrome protein (WASP) | Src | TYROSINE KINASE-ACTIVITY | 11Q13 AMPLIFICATION | family verprolin homologous (WAVE) | actin-related protein (Arp2/3) complex | PRIMARY BREAST-CANCER | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | ARP2/3 COMPLEX | MODULATE CELL-SHAPE | suppressor of cAMP receptor (SCAR)/WASP | ALDRICH-SYNDROME PROTEIN | TIGHT JUNCTION | cell motility | endocytosis | N-WASP | EXTRACELLULAR-MATRIX | Cortactin | Signal Transduction - physiology | Animals | Actins - physiology | Humans | Microfilament Proteins - physiology | SH, Src homology | 3) complex | WH, WASP homology | EGF, epidermal growth factor | SCAR, suppressor of cAMP receptor | WIP, WASP-interacting protein | NTA, N-terminal acidic (domain) | actin-related protein (Arp2 | GBD, GTPase binding domain | WAVE, WASP family verprolin homologous | PDZ, PSD-95 | WCA, WH2-central–acidic region | Wiskott–Aldrich syndrome protein (WASP) | Hip1R, Huntingtin-interacting protein 1-related | GST, glutathione S-transferase | EVH1, Ena VASP homology 1 | WASP family verprolin homologous (WAVE) | GK(AP), guanylate kinase (associated protein) | HS1, haematopoietic lineage cell-specific protein 1 | ZO-1 | PDGF, platelet-derived growth factor | Dlg | Fgd1, faciogenital dysplasia 1 | NPF, nucleation promoting factor | CortBP1, cortactin binding protein 1 | Arp, actin-related protein | CD2AP, CD2-associated protein | Review | EC MLCK, endothelial cell myosin light-chain kinase | ERK kinase | suppressor of cAMP receptor (SCAR) | WASP, Wiskott–Aldrich syndrome protein | EHEC, enterohaemorrhagic Escherichia coli | N-WASP, neural WASP | PIP2, phosphatidylinositol 4,5 bisphosphate | MEK, MAP kinase | Abp1, actin-binding protein 1 | PAK, p21-activated kinase | ADF-H, actin depolymerizing factor homology | NMDA, N-methyl-D-aspartate | EPEC, enteropathogenic E. coli | ZO-1, zonnula occludens 1 | PSD, post-synaptic density | GEF, guanine nucleotide exchange factor | HP, helical and proline-rich (region) | HGF, hepatocyte growth factor | CCND1, cell cycle regulatory protein cyclin D1
Actin-related protein (Arp2/3) complex | Cell motility | Endocytosis | Suppressor of cAMP receptor (SCAR)/WASP family verprolin homologous (WAVE) | Wiskott-Aldrich syndrome protein (WASP) | Src | TYROSINE KINASE-ACTIVITY | 11Q13 AMPLIFICATION | family verprolin homologous (WAVE) | actin-related protein (Arp2/3) complex | PRIMARY BREAST-CANCER | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | ARP2/3 COMPLEX | MODULATE CELL-SHAPE | suppressor of cAMP receptor (SCAR)/WASP | ALDRICH-SYNDROME PROTEIN | TIGHT JUNCTION | cell motility | endocytosis | N-WASP | EXTRACELLULAR-MATRIX | Cortactin | Signal Transduction - physiology | Animals | Actins - physiology | Humans | Microfilament Proteins - physiology | SH, Src homology | 3) complex | WH, WASP homology | EGF, epidermal growth factor | SCAR, suppressor of cAMP receptor | WIP, WASP-interacting protein | NTA, N-terminal acidic (domain) | actin-related protein (Arp2 | GBD, GTPase binding domain | WAVE, WASP family verprolin homologous | PDZ, PSD-95 | WCA, WH2-central–acidic region | Wiskott–Aldrich syndrome protein (WASP) | Hip1R, Huntingtin-interacting protein 1-related | GST, glutathione S-transferase | EVH1, Ena VASP homology 1 | WASP family verprolin homologous (WAVE) | GK(AP), guanylate kinase (associated protein) | HS1, haematopoietic lineage cell-specific protein 1 | ZO-1 | PDGF, platelet-derived growth factor | Dlg | Fgd1, faciogenital dysplasia 1 | NPF, nucleation promoting factor | CortBP1, cortactin binding protein 1 | Arp, actin-related protein | CD2AP, CD2-associated protein | Review | EC MLCK, endothelial cell myosin light-chain kinase | ERK kinase | suppressor of cAMP receptor (SCAR) | WASP, Wiskott–Aldrich syndrome protein | EHEC, enterohaemorrhagic Escherichia coli | N-WASP, neural WASP | PIP2, phosphatidylinositol 4,5 bisphosphate | MEK, MAP kinase | Abp1, actin-binding protein 1 | PAK, p21-activated kinase | ADF-H, actin depolymerizing factor homology | NMDA, N-methyl-D-aspartate | EPEC, enteropathogenic E. coli | ZO-1, zonnula occludens 1 | PSD, post-synaptic density | GEF, guanine nucleotide exchange factor | HP, helical and proline-rich (region) | HGF, hepatocyte growth factor | CCND1, cell cycle regulatory protein cyclin D1
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 08/2011, Volume 108, Issue 33, pp. E463 - E471
Actin-related protein (Arp) 2/3 complex mediates the formation of actin filament branches during endocytosis and at the leading edge of motile cells. The...
Polymerization | Thermodynamics | Crystallography | polymerization | ACTIVATION | PHAGOCYTOSIS | CYTOSKELETON | MULTIDISCIPLINARY SCIENCES | thermodynamics | FAMILY PROTEINS | ALDRICH-SYNDROME PROTEIN | CDC42 | crystallography | WASP/SCAR PROTEINS | ACTIN-BASED MOTILITY | N-WASP | Cattle - metabolism | Schizosaccharomyces pombe Proteins - chemistry | Schizosaccharomyces - chemistry | Actin-Related Protein 2 - chemistry | Crystallography, X-Ray | Actin-Related Protein 3 - chemistry | Schizosaccharomyces - metabolism | Animals | Wiskott-Aldrich Syndrome Protein - chemistry | Protein Structure, Quaternary | Schizosaccharomyces pombe Proteins - metabolism | Actin-Related Protein 3 - metabolism | Wiskott-Aldrich Syndrome Protein - metabolism | Actin-Related Protein 2 - metabolism | Protein Interaction Domains and Motifs | Binding Sites | ACTIN | BASIC BIOLOGICAL SCIENCES | CATTLE | STOICHIOMETRY | CROSS-LINKING | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | POLYMERIZATION | 60 APPLIED LIFE SCIENCES | THERMODYNAMICS | AFFINITY | CALORIMETRY | YEASTS | FISSION | PROTEINS | TITRATION | Biological Sciences | PNAS Plus
Polymerization | Thermodynamics | Crystallography | polymerization | ACTIVATION | PHAGOCYTOSIS | CYTOSKELETON | MULTIDISCIPLINARY SCIENCES | thermodynamics | FAMILY PROTEINS | ALDRICH-SYNDROME PROTEIN | CDC42 | crystallography | WASP/SCAR PROTEINS | ACTIN-BASED MOTILITY | N-WASP | Cattle - metabolism | Schizosaccharomyces pombe Proteins - chemistry | Schizosaccharomyces - chemistry | Actin-Related Protein 2 - chemistry | Crystallography, X-Ray | Actin-Related Protein 3 - chemistry | Schizosaccharomyces - metabolism | Animals | Wiskott-Aldrich Syndrome Protein - chemistry | Protein Structure, Quaternary | Schizosaccharomyces pombe Proteins - metabolism | Actin-Related Protein 3 - metabolism | Wiskott-Aldrich Syndrome Protein - metabolism | Actin-Related Protein 2 - metabolism | Protein Interaction Domains and Motifs | Binding Sites | ACTIN | BASIC BIOLOGICAL SCIENCES | CATTLE | STOICHIOMETRY | CROSS-LINKING | CRYSTAL STRUCTURE | CRYSTALLOGRAPHY | POLYMERIZATION | 60 APPLIED LIFE SCIENCES | THERMODYNAMICS | AFFINITY | CALORIMETRY | YEASTS | FISSION | PROTEINS | TITRATION | Biological Sciences | PNAS Plus
Journal Article
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Full Text
Phase transitions of multivalent proteins can promote clustering of membrane receptors
eLife, ISSN 2050-084X, 2014, Volume 3
Clustering of proteins into micrometer-sized structures at membranes is observed in many signaling pathways. Most models of clustering are specific to...
polymerization | phase separation
polymerization | phase separation