PLoS Biology, ISSN 1544-9173, 2005, Volume 3, Issue 11, pp. 1902 - 1909
Actin branch junctions are conserved cytoskeletal elements critical for the generation of protrusive force during actin polymerization- driven cellular...
CORTACTIN PROMOTES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | BIOLOGY | RECONSTRUCTIONS | ELECTRON-MICROSCOPY | STATE | N-WASP | PROTEINS | ATOMIC MODELS | MOTILITY | Fungal Proteins - chemistry | Open Reading Frames | Bacterial Proteins - chemistry | Molecular Sequence Data | Actins - chemistry | Luminescent Proteins - chemistry | Green Fluorescent Proteins - chemistry | Muscles - metabolism | Dimerization | Protein Structure, Tertiary | Dendrites - metabolism | Microfilament Proteins - chemistry | Rabbits | Actin-Related Protein 2 - chemistry | Actin-Related Protein 3 - chemistry | Cytoskeletal Proteins - chemistry | Genetic Techniques | Microscopy, Electron | Plasmids - metabolism | Animals | Pyrenes - chemistry | Image Processing, Computer-Assisted | Protein Binding | Software | In Vitro Techniques | In Vitro | Molecular Biology | Bioinformatics | Structural Biology | Computational Biology | Cell Biology | Proteins | Maps | Motility | Microscopy | Molecular weight
CORTACTIN PROMOTES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | BIOLOGY | RECONSTRUCTIONS | ELECTRON-MICROSCOPY | STATE | N-WASP | PROTEINS | ATOMIC MODELS | MOTILITY | Fungal Proteins - chemistry | Open Reading Frames | Bacterial Proteins - chemistry | Molecular Sequence Data | Actins - chemistry | Luminescent Proteins - chemistry | Green Fluorescent Proteins - chemistry | Muscles - metabolism | Dimerization | Protein Structure, Tertiary | Dendrites - metabolism | Microfilament Proteins - chemistry | Rabbits | Actin-Related Protein 2 - chemistry | Actin-Related Protein 3 - chemistry | Cytoskeletal Proteins - chemistry | Genetic Techniques | Microscopy, Electron | Plasmids - metabolism | Animals | Pyrenes - chemistry | Image Processing, Computer-Assisted | Protein Binding | Software | In Vitro Techniques | In Vitro | Molecular Biology | Bioinformatics | Structural Biology | Computational Biology | Cell Biology | Proteins | Maps | Motility | Microscopy | Molecular weight
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 09/2013, Volume 20, Issue 9, pp. 1062 - 1068
The Arp2/3 complex mediates formation of complex cellular structures such as lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is...
FACTOR HOMOLOGY DOMAIN | ACTIN POLYMERIZATION | CRYSTAL-STRUCTURE | CORTACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILY | CELL BIOLOGY | WASP/SCAR PROTEINS | INHIBITION | BIOPHYSICS | N-WASP | BINDING | ATP | Protein Subunits | Glia Maturation Factor - genetics | Actins - metabolism | Molecular Sequence Data | Actin-Related Protein 2-3 Complex - genetics | Crystallography, X-Ray | Wiskott-Aldrich Syndrome Protein Family - chemistry | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cattle | Actins - chemistry | Protein Interaction Domains and Motifs | Glia Maturation Factor - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Wiskott-Aldrich Syndrome Protein Family - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Actin-Related Protein 2-3 Complex - chemistry | Sequence Homology, Amino Acid | Multiprotein Complexes - chemistry | Animals | Glia Maturation Factor - metabolism | Mice | Physiological aspects | Glial cell line-derived neurotrophic factor | Research | Muscle proteins | Structure | Proteins | Molecular biology | Binding sites | Crystal structure
FACTOR HOMOLOGY DOMAIN | ACTIN POLYMERIZATION | CRYSTAL-STRUCTURE | CORTACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILY | CELL BIOLOGY | WASP/SCAR PROTEINS | INHIBITION | BIOPHYSICS | N-WASP | BINDING | ATP | Protein Subunits | Glia Maturation Factor - genetics | Actins - metabolism | Molecular Sequence Data | Actin-Related Protein 2-3 Complex - genetics | Crystallography, X-Ray | Wiskott-Aldrich Syndrome Protein Family - chemistry | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cattle | Actins - chemistry | Protein Interaction Domains and Motifs | Glia Maturation Factor - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Wiskott-Aldrich Syndrome Protein Family - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Actin-Related Protein 2-3 Complex - chemistry | Sequence Homology, Amino Acid | Multiprotein Complexes - chemistry | Animals | Glia Maturation Factor - metabolism | Mice | Physiological aspects | Glial cell line-derived neurotrophic factor | Research | Muscle proteins | Structure | Proteins | Molecular biology | Binding sites | Crystal structure
Journal Article
European Journal of Cell Biology, ISSN 0171-9335, 10/2017, Volume 96, Issue 7, pp. 673 - 684
Cellular distribution of invadopodia is regulated by nanometer scale surface protein patterns. Asteriks show significant differences between different surfaces...
Cortactin | Invadopodia | Nanopattern | Electron beam lithography | Golgi complex | Nanopattem | METALLOPROTEINASE | TUMOR CELLS | CELL BIOLOGY | BREAST-CANCER CELLS | ADHESION | DEGRADATION | PODOSOMES | EXTRACELLULAR-MATRIX | N-WASP | INVASIVE CELLS | Cell Adhesion - genetics | Nanoparticles - chemistry | Cortactin - chemistry | Humans | Tomography, X-Ray Computed | Extracellular Matrix - chemistry | Laminin - genetics | Extracellular Matrix - genetics | Caseins - chemistry | Fibronectins - chemistry | Neoplasms - genetics | Cell Line, Tumor | Laminin - chemistry | Fibronectins - genetics | Neoplasms - pathology | Podosomes - genetics | Golgi Apparatus - genetics | Podosomes - chemistry | Fibronectins | Casein | Laminin
Cortactin | Invadopodia | Nanopattern | Electron beam lithography | Golgi complex | Nanopattem | METALLOPROTEINASE | TUMOR CELLS | CELL BIOLOGY | BREAST-CANCER CELLS | ADHESION | DEGRADATION | PODOSOMES | EXTRACELLULAR-MATRIX | N-WASP | INVASIVE CELLS | Cell Adhesion - genetics | Nanoparticles - chemistry | Cortactin - chemistry | Humans | Tomography, X-Ray Computed | Extracellular Matrix - chemistry | Laminin - genetics | Extracellular Matrix - genetics | Caseins - chemistry | Fibronectins - chemistry | Neoplasms - genetics | Cell Line, Tumor | Laminin - chemistry | Fibronectins - genetics | Neoplasms - pathology | Podosomes - genetics | Golgi Apparatus - genetics | Podosomes - chemistry | Fibronectins | Casein | Laminin
Journal Article
Journal of biological chemistry, ISSN 0021-9258, 2010, Volume 285, Issue 24, pp. 18672 - 18683
We here identify protein kinase D (PKD) as an upstream regulator of the F-actin-binding protein cortactin and the Arp actin polymerization machinery. PKD...
CARCINOMA-CELLS | MIGRATION | F-ACTIN | COFILIN-PHOSPHATASE SLINGSHOT | LEADING-EDGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SITES | LAMELLIPODIA | ARP2/3 COMPLEX | N-WASP | C-MU | Cell Line | Phosphorylation | Cortactin - chemistry | Humans | Wiskott-Aldrich Syndrome Protein Family - chemistry | Neuregulin-1 - chemistry | Amino Acid Motifs | Immunohistochemistry - methods | Protein Kinase C - chemistry | Actins - chemistry | Cell Line, Tumor | Fluorescence Resonance Energy Transfer | Protein Binding | Cell Movement | Cell Migration | Cortactin | WAVE | Signal Transduction | Protein Kinases | Actin | Cell Motility | Protein Phosphorylation | Arp | Cell Biology
CARCINOMA-CELLS | MIGRATION | F-ACTIN | COFILIN-PHOSPHATASE SLINGSHOT | LEADING-EDGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SITES | LAMELLIPODIA | ARP2/3 COMPLEX | N-WASP | C-MU | Cell Line | Phosphorylation | Cortactin - chemistry | Humans | Wiskott-Aldrich Syndrome Protein Family - chemistry | Neuregulin-1 - chemistry | Amino Acid Motifs | Immunohistochemistry - methods | Protein Kinase C - chemistry | Actins - chemistry | Cell Line, Tumor | Fluorescence Resonance Energy Transfer | Protein Binding | Cell Movement | Cell Migration | Cortactin | WAVE | Signal Transduction | Protein Kinases | Actin | Cell Motility | Protein Phosphorylation | Arp | Cell Biology
Journal Article
Chemical Communications, ISSN 1359-7345, 06/2013, Volume 49, Issue 47, pp. 5387 - 5389
A bi-functional peptide is designed to incorporate protein recognition and signal amplification functions into a single short peptide sequence.
RECOGNITION MODULES | IONS | CHEMISTRY, MULTIDISCIPLINARY | Placenta - metabolism | Pregnancy | Proteins | Copper - chemistry | Peptides - chemistry | Cortactin - chemistry | Humans | Female | Cortactin - metabolism | Coordination Complexes - chemistry
RECOGNITION MODULES | IONS | CHEMISTRY, MULTIDISCIPLINARY | Placenta - metabolism | Pregnancy | Proteins | Copper - chemistry | Peptides - chemistry | Cortactin - chemistry | Humans | Female | Cortactin - metabolism | Coordination Complexes - chemistry
Journal Article
Biophysical Journal, ISSN 0006-3495, 2008, Volume 95, Issue 2, pp. 886 - 894
Disruption of pulmonary endothelial cell (EC) barrier function is a critical pathophysiologic event in highly morbid inflammatory conditions such as sepsis and...
ATOMIC-FORCE MICROSCOPY | BIOPHYSICS | INTEGRITY | CELL BARRIER ENHANCEMENT | FIXATION | SPHINGOSINE 1-PHOSPHATE | REAL-TIME | Pulmonary Artery - chemistry | Cortactin - chemistry | Lysophospholipids - chemistry | Sphingosine - physiology | Humans | Elasticity | Stress, Mechanical | Thrombin - physiology | Endothelium, Vascular - chemistry | Endothelium, Vascular - physiology | Pulmonary Artery - physiology | Sphingosine - analogs & derivatives | Thrombin - chemistry | Actins - chemistry | Microscopy, Atomic Force - methods | Lysophospholipids - physiology | Actins - physiology | Cortactin - physiology | Sphingosine - chemistry | Phosphates | Atomic force microscopy | Analysis | Sphingosine | Thrombin | Permeability | Binding proteins | Muscle proteins | Protein binding | Endothelium | Pathology | Cytoskeleton | Respiratory distress syndrome | Cells | Control | Elevated | Barriers | Arteries | Cell Biophysics
ATOMIC-FORCE MICROSCOPY | BIOPHYSICS | INTEGRITY | CELL BARRIER ENHANCEMENT | FIXATION | SPHINGOSINE 1-PHOSPHATE | REAL-TIME | Pulmonary Artery - chemistry | Cortactin - chemistry | Lysophospholipids - chemistry | Sphingosine - physiology | Humans | Elasticity | Stress, Mechanical | Thrombin - physiology | Endothelium, Vascular - chemistry | Endothelium, Vascular - physiology | Pulmonary Artery - physiology | Sphingosine - analogs & derivatives | Thrombin - chemistry | Actins - chemistry | Microscopy, Atomic Force - methods | Lysophospholipids - physiology | Actins - physiology | Cortactin - physiology | Sphingosine - chemistry | Phosphates | Atomic force microscopy | Analysis | Sphingosine | Thrombin | Permeability | Binding proteins | Muscle proteins | Protein binding | Endothelium | Pathology | Cytoskeleton | Respiratory distress syndrome | Cells | Control | Elevated | Barriers | Arteries | Cell Biophysics
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2016, Volume 11, Issue 2, p. e0148996
The proto-oncogene c-Src is involved in a variety of signaling processes. Therefore, c-Src spatiotemporal localization is critical for interaction with...
SURVIVAL | CELLS | ACTIVATION | METASTASIS | MEMBRANE | MULTIDISCIPLINARY SCIENCES | KINASE | RESISTANCE | SIGNALS | CANCER | RHOB | Cell Line | Green Fluorescent Proteins - metabolism | Signal Transduction | Wiskott-Aldrich Syndrome Protein Family - metabolism | Humans | Actins - metabolism | Rats | Cytoplasm - metabolism | Cortactin - metabolism | rhoB GTP-Binding Protein - metabolism | Nocodazole - chemistry | Fibronectins - metabolism | Protein Transport | Microscopy, Confocal | Microtubules - metabolism | Animals | Fibronectins - chemistry | Time Factors | src-Family Kinases - metabolism | Actins - chemistry | Polymers - chemistry | Rho Guanine Nucleotide Exchange Factors - metabolism | Retinal Pigment Epithelium - cytology | Cell Movement | Polymerization | Muscle proteins | Actin | Molecular machines | Growth cones | Medical research | Membranes | GTP | Downstream effects | Developmental biology | Trafficking | Thyroid gland | Metastasis | Kinases | Src protein | Cell adhesion & migration | Depolymerization | Vesicles | Cones | Microtubules | Infrared imaging systems | Molecular biology | Localization | Guanosinetriphosphatase
SURVIVAL | CELLS | ACTIVATION | METASTASIS | MEMBRANE | MULTIDISCIPLINARY SCIENCES | KINASE | RESISTANCE | SIGNALS | CANCER | RHOB | Cell Line | Green Fluorescent Proteins - metabolism | Signal Transduction | Wiskott-Aldrich Syndrome Protein Family - metabolism | Humans | Actins - metabolism | Rats | Cytoplasm - metabolism | Cortactin - metabolism | rhoB GTP-Binding Protein - metabolism | Nocodazole - chemistry | Fibronectins - metabolism | Protein Transport | Microscopy, Confocal | Microtubules - metabolism | Animals | Fibronectins - chemistry | Time Factors | src-Family Kinases - metabolism | Actins - chemistry | Polymers - chemistry | Rho Guanine Nucleotide Exchange Factors - metabolism | Retinal Pigment Epithelium - cytology | Cell Movement | Polymerization | Muscle proteins | Actin | Molecular machines | Growth cones | Medical research | Membranes | GTP | Downstream effects | Developmental biology | Trafficking | Thyroid gland | Metastasis | Kinases | Src protein | Cell adhesion & migration | Depolymerization | Vesicles | Cones | Microtubules | Infrared imaging systems | Molecular biology | Localization | Guanosinetriphosphatase
Journal Article
Cytoskeleton, ISSN 1949-3584, 10/2015, Volume 72, Issue 10, pp. 542 - 556
It remains a challenge to decode the molecular basis of the long‐term actin cytoskeleton rearrangements that are governed by the reprogramming of gene...
actin cytoskeleton | Bacillus anthracis toxin | HAT | vascular permeability | gene expression | HDAC | Actin cytoskeleton | Gene expression | Vascular permeability | LASER NANOSURGERY | CYTOSKELETON | CORTACTIN | INDUCTION | CELL BIOLOGY | STRESS FIBERS | MECHANICS | ENDOTHELIAL-CELLS | IN-VIVO | ADHERENS JUNCTIONS | PROTEINS | Human Umbilical Vein Endothelial Cells | Tensile Strength | Antigens, Bacterial - chemistry | Histones - chemistry | Humans | Gene Expression Regulation | Cell Communication | Hydroxamic Acids - chemistry | Bacterial Toxins - chemistry | Cell Nucleus - metabolism | Endothelial Cells - cytology | Light | Actins - chemistry | Adherens Junctions | Stress Fibers - chemistry | Acetylation | Microscopy, Fluorescence | Bacillus anthracis - chemistry
actin cytoskeleton | Bacillus anthracis toxin | HAT | vascular permeability | gene expression | HDAC | Actin cytoskeleton | Gene expression | Vascular permeability | LASER NANOSURGERY | CYTOSKELETON | CORTACTIN | INDUCTION | CELL BIOLOGY | STRESS FIBERS | MECHANICS | ENDOTHELIAL-CELLS | IN-VIVO | ADHERENS JUNCTIONS | PROTEINS | Human Umbilical Vein Endothelial Cells | Tensile Strength | Antigens, Bacterial - chemistry | Histones - chemistry | Humans | Gene Expression Regulation | Cell Communication | Hydroxamic Acids - chemistry | Bacterial Toxins - chemistry | Cell Nucleus - metabolism | Endothelial Cells - cytology | Light | Actins - chemistry | Adherens Junctions | Stress Fibers - chemistry | Acetylation | Microscopy, Fluorescence | Bacillus anthracis - chemistry
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 01/2018, Volume 495, Issue 1, pp. 1522 - 1527
Tyrosine kinases are important enzymes that mediate signal transduction at the plasma membrane. While the significance of membrane localization of tyrosine...
Intrinsically disordered region | F-BAR domain | Fer | Phosphorylation | Membrane curvature | tyrosine kinase | BIOPHYSICS | CORTACTIN PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | PROTEINS | Fer tyrosine kinase | Cell Membrane - chemistry | Intrinsically Disordered Proteins - chemistry | Protein-Tyrosine Kinases - chemistry | Protein Binding | Protein-Tyrosine Kinases - ultrastructure | Protein Conformation | Cell Membrane - ultrastructure | Lipid Bilayers - chemistry | Membrane Fluidity | Binding Sites | Intrinsically Disordered Proteins - ultrastructure | Tyrosine | Enzymes | Medical colleges | Analysis | Phenols | Cellular signal transduction | Molecular biology
Intrinsically disordered region | F-BAR domain | Fer | Phosphorylation | Membrane curvature | tyrosine kinase | BIOPHYSICS | CORTACTIN PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | PROTEINS | Fer tyrosine kinase | Cell Membrane - chemistry | Intrinsically Disordered Proteins - chemistry | Protein-Tyrosine Kinases - chemistry | Protein Binding | Protein-Tyrosine Kinases - ultrastructure | Protein Conformation | Cell Membrane - ultrastructure | Lipid Bilayers - chemistry | Membrane Fluidity | Binding Sites | Intrinsically Disordered Proteins - ultrastructure | Tyrosine | Enzymes | Medical colleges | Analysis | Phenols | Cellular signal transduction | Molecular biology
Journal Article
Amino Acids, ISSN 0939-4451, 2/2013, Volume 44, Issue 2, pp. 607 - 614
SH3 domains are probably the most abundant molecular-recognition modules of the proteome. A common feature of these domains is their interaction with ligand...
Life Sciences | Biochemistry, general | Cortactin | Analytical Chemistry | Life Sciences, general | Pro-rich peptides | Biochemical Engineering | Proteomics | Neurobiology | 4-R-Fluoroproline | 4-R-Hydroxyproline | Protein–protein interaction | Protein-protein interaction | Amino Acid Sequence | Peptides - chemistry | Proline - analogs & derivatives | Protein Structure, Secondary | Cortactin - chemistry | Proline - metabolism | Hydroxyproline - metabolism | Molecular Conformation | Molecular Sequence Data | Cortactin - metabolism | Amino Acid Motifs | Proline - chemistry | src Homology Domains | Animals | Peptides - metabolism | Protein Binding | Mice | Protein-Serine-Threonine Kinases - chemistry | Kinetics | Hydroxyproline - chemistry | Protein-Serine-Threonine Kinases - metabolism
Life Sciences | Biochemistry, general | Cortactin | Analytical Chemistry | Life Sciences, general | Pro-rich peptides | Biochemical Engineering | Proteomics | Neurobiology | 4-R-Fluoroproline | 4-R-Hydroxyproline | Protein–protein interaction | Protein-protein interaction | Amino Acid Sequence | Peptides - chemistry | Proline - analogs & derivatives | Protein Structure, Secondary | Cortactin - chemistry | Proline - metabolism | Hydroxyproline - metabolism | Molecular Conformation | Molecular Sequence Data | Cortactin - metabolism | Amino Acid Motifs | Proline - chemistry | src Homology Domains | Animals | Peptides - metabolism | Protein Binding | Mice | Protein-Serine-Threonine Kinases - chemistry | Kinetics | Hydroxyproline - chemistry | Protein-Serine-Threonine Kinases - metabolism
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2895 - 14
Formation and turnover of branched actin networks underlies cell migration and other essential force-driven processes. Type I nucleation-promoting factors...
CONFORMATIONAL-CHANGES | PROTEIN | YEAST ACTIN | STRUCTURAL BASIS | SINGLE-MOLECULE | CORTACTIN | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | FILAMENT NETWORK FORMATION | 2 BINDING-SITES | N-WASP | Glia Maturation Factor - genetics | Saccharomyces cerevisiae - genetics | Protein Multimerization | Actins - metabolism | Actin-Related Protein 2-3 Complex - genetics | Actins - genetics | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Microfilament Proteins - metabolism | Glia Maturation Factor - chemistry | Microfilament Proteins - genetics | Microfilament Proteins - chemistry | Microscopy, Electron, Transmission | Actin Cytoskeleton - metabolism | Models, Molecular | Saccharomyces cerevisiae Proteins - genetics | Actin-Related Protein 2-3 Complex - chemistry | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Glia Maturation Factor - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Yeast | Nucleation | Filaments | Actin | Dimers | Cell migration | Monomers | Molecular chains | Cell adhesion & migration
CONFORMATIONAL-CHANGES | PROTEIN | YEAST ACTIN | STRUCTURAL BASIS | SINGLE-MOLECULE | CORTACTIN | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | FILAMENT NETWORK FORMATION | 2 BINDING-SITES | N-WASP | Glia Maturation Factor - genetics | Saccharomyces cerevisiae - genetics | Protein Multimerization | Actins - metabolism | Actin-Related Protein 2-3 Complex - genetics | Actins - genetics | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Microfilament Proteins - metabolism | Glia Maturation Factor - chemistry | Microfilament Proteins - genetics | Microfilament Proteins - chemistry | Microscopy, Electron, Transmission | Actin Cytoskeleton - metabolism | Models, Molecular | Saccharomyces cerevisiae Proteins - genetics | Actin-Related Protein 2-3 Complex - chemistry | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Glia Maturation Factor - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Yeast | Nucleation | Filaments | Actin | Dimers | Cell migration | Monomers | Molecular chains | Cell adhesion & migration
Journal Article
Molecular Cell, ISSN 1097-2765, 2007, Volume 27, Issue 2, pp. 197 - 213
Histone deacetylase 6 (HDAC6) is a tubulin-specific deacetylase that regulates microtubule-dependent cell movement. In this study, we identify the...
CELLBIO | PROTEINS | COMPLEX | DOMAIN | POLYUBIQUITIN | MICROTUBULES | DEACETYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | RAC1 | TUBULIN | STRESS | BINDING | CELL BIOLOGY | NIH 3T3 Cells | p300-CBP Transcription Factors | Cortactin - chemistry | Humans | Actins - metabolism | Molecular Sequence Data | Cell Movement - physiology | Repetitive Sequences, Amino Acid | Histone Acetyltransferases - metabolism | Acetylation | Recombinant Proteins - metabolism | Amino Acid Sequence | Rabbits | Mutagenesis, Site-Directed | Histone Deacetylases - genetics | Histone Deacetylase 6 | Cell Cycle Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Histone Deacetylases - metabolism | Recombinant Proteins - genetics | Cortactin - metabolism | Sequence Homology, Amino Acid | Transcription Factors - metabolism | Animals | Cortactin - genetics | Protein Binding | Histone Deacetylase Inhibitors | Mice | HeLa Cells | In Vitro Techniques | Amino Acid Substitution
CELLBIO | PROTEINS | COMPLEX | DOMAIN | POLYUBIQUITIN | MICROTUBULES | DEACETYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | RAC1 | TUBULIN | STRESS | BINDING | CELL BIOLOGY | NIH 3T3 Cells | p300-CBP Transcription Factors | Cortactin - chemistry | Humans | Actins - metabolism | Molecular Sequence Data | Cell Movement - physiology | Repetitive Sequences, Amino Acid | Histone Acetyltransferases - metabolism | Acetylation | Recombinant Proteins - metabolism | Amino Acid Sequence | Rabbits | Mutagenesis, Site-Directed | Histone Deacetylases - genetics | Histone Deacetylase 6 | Cell Cycle Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Histone Deacetylases - metabolism | Recombinant Proteins - genetics | Cortactin - metabolism | Sequence Homology, Amino Acid | Transcription Factors - metabolism | Animals | Cortactin - genetics | Protein Binding | Histone Deacetylase Inhibitors | Mice | HeLa Cells | In Vitro Techniques | Amino Acid Substitution
Journal Article
Current Biology, ISSN 0960-9822, 11/2013, Volume 23, Issue 21, pp. 2079 - 2089
Tks5 regulates invadopodium formation, but the precise timing during invadopodium lifetime (initiation, stabilization, maturation) when Tks5 plays a role is...
CANCER-CELLS | I-ALPHA | INVASION | MATRIX DEGRADATION | INOSITOL 5-PHOSPHATASE SHIP2 | CORTACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-WASP-ARP2/3 COMPLEX | N-WASP | ADAPTER PROTEIN | PODOSOME FORMATION | CELL BIOLOGY | Phosphoric Monoester Hydrolases - genetics | Cell Surface Extensions - metabolism | Humans | Adaptor Proteins, Vesicular Transport - genetics | Inositol Polyphosphate 5-Phosphatases | Adaptor Proteins, Vesicular Transport - metabolism | Breast Neoplasms - metabolism | Breast Neoplasms - pathology | Neoplasm Metastasis - pathology | Biosensing Techniques | Female | Adaptor Proteins, Vesicular Transport - chemistry | Microfilament Proteins - metabolism | Phosphoric Monoester Hydrolases - metabolism | Cell Movement | Phosphoric Monoester Hydrolases - chemistry | Breast cancer
CANCER-CELLS | I-ALPHA | INVASION | MATRIX DEGRADATION | INOSITOL 5-PHOSPHATASE SHIP2 | CORTACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-WASP-ARP2/3 COMPLEX | N-WASP | ADAPTER PROTEIN | PODOSOME FORMATION | CELL BIOLOGY | Phosphoric Monoester Hydrolases - genetics | Cell Surface Extensions - metabolism | Humans | Adaptor Proteins, Vesicular Transport - genetics | Inositol Polyphosphate 5-Phosphatases | Adaptor Proteins, Vesicular Transport - metabolism | Breast Neoplasms - metabolism | Breast Neoplasms - pathology | Neoplasm Metastasis - pathology | Biosensing Techniques | Female | Adaptor Proteins, Vesicular Transport - chemistry | Microfilament Proteins - metabolism | Phosphoric Monoester Hydrolases - metabolism | Cell Movement | Phosphoric Monoester Hydrolases - chemistry | Breast cancer
Journal Article
Traffic, ISSN 1398-9219, 11/2007, Volume 8, Issue 11, pp. 1465 - 1475
Membrane trafficking and remodeling of the actin cytoskeleton are critical activities contributing to cellular events that include cell growth, migration and...
focal adhesion | podosome | actin | invadopodia | Arf1 | EGF receptor | ASAP1 | Arf6 | circular dorsal ruffles | cortactin | Cortactin | Circular dorsal ruffles | Actin | Podosome | Focal adhesion | Invadopodia | GTPASE-ACTIVATING-PROTEIN | PAXILLIN-BINDING PROTEIN | FOCAL ADHESIONS | CELL BIOLOGY | CELL-MIGRATION | EPIDERMAL-GROWTH-FACTOR | MEMBRANE CURVATURE | COPI VESICLES | CANCER INVASIVE ACTIVITIES | ACTIN CYTOSKELETON | ADAPTER PROTEIN | Protein Structure, Tertiary | Signal Transduction | Humans | Actins - metabolism | Adenosine Diphosphate - chemistry | Guanosine Triphosphate - metabolism | Protein Interaction Mapping | Hydrolysis | ADP-Ribosylation Factors - chemistry | Lipids - chemistry | Receptor, Epidermal Growth Factor - metabolism | Animals | Models, Biological | Actins - chemistry | Cytoskeleton - metabolism | Protein Binding | ADP-Ribosylation Factors - physiology | Cell Membrane - metabolism | Guanosine Triphosphate - chemistry | GTP-Binding Proteins - metabolism | Proteins | Physiological aspects | Polypeptides
focal adhesion | podosome | actin | invadopodia | Arf1 | EGF receptor | ASAP1 | Arf6 | circular dorsal ruffles | cortactin | Cortactin | Circular dorsal ruffles | Actin | Podosome | Focal adhesion | Invadopodia | GTPASE-ACTIVATING-PROTEIN | PAXILLIN-BINDING PROTEIN | FOCAL ADHESIONS | CELL BIOLOGY | CELL-MIGRATION | EPIDERMAL-GROWTH-FACTOR | MEMBRANE CURVATURE | COPI VESICLES | CANCER INVASIVE ACTIVITIES | ACTIN CYTOSKELETON | ADAPTER PROTEIN | Protein Structure, Tertiary | Signal Transduction | Humans | Actins - metabolism | Adenosine Diphosphate - chemistry | Guanosine Triphosphate - metabolism | Protein Interaction Mapping | Hydrolysis | ADP-Ribosylation Factors - chemistry | Lipids - chemistry | Receptor, Epidermal Growth Factor - metabolism | Animals | Models, Biological | Actins - chemistry | Cytoskeleton - metabolism | Protein Binding | ADP-Ribosylation Factors - physiology | Cell Membrane - metabolism | Guanosine Triphosphate - chemistry | GTP-Binding Proteins - metabolism | Proteins | Physiological aspects | Polypeptides
Journal Article