FEBS Letters, ISSN 0014-5793, 12/2015, Volume 589, Issue 24, pp. 3760 - 3772
Glial cell line-derived neurotrophic factor (GDNF) and its canonical receptor Ret can signal together or independently to fulfill many important functions in...
Rearranged during transfection | Parkinson disease | Drug addiction | Mouse model | Dopaminergic system | Glia cell line-derived neurotrophic factor | MAOA/MAOB | orphan nuclear receptor and transcription factor | cytoplasmic SH2 domain containing protein tyrosine phosphatase | Ras | RRF | COMT | PTEN-induced putative kinase 1 | SH3 and multiple ankyrin repeat domains 3, proline-rich synapse-associated protein 2 (ProSAP2) | PI3K | sorting protein-related receptor with A-type repeats, a member of the mammal Vps10p domain receptor | subunits of the Ca2+-sensitive, voltage gated A-type K+ channel | SH2 domain containing transforming protein 1 | Nurr1 | proprotein convertases | protein kinase B, serine/threonine-specific protein kinase | calcium-calmodulin-dependent protein kinase II β isoform | FRS2 | phosphatase and tensin homolog | catecholamine | SHP-2 | growth factor receptor-bound protein 2, 7 and 10, adaptor proteins | fibroblast growth factor receptor substrate 2, adaptor protein | monoamine oxidases A and B | carbonyl cyanide m-chlorophenyl hydrazone | ERK | brain derived neurotrophic factor | deglycase, oxidative stress sensor and redox-sensitive chaperone and protease | VTA | tyrosines, which can be phosphorylated | cAMP | extracellular-signal-regulated kinases, classical MAPKs | CaMKIIβ | Kv4.3 and KChip3 | GRB2/7/10 | Ser/Thr | SNP | endoplasmatic reticulum | nerve growth factor | monoamine, neurotransmitter type including dopamine, epinephrine (adrenaline) and norepinephrine (noradrenaline) | TGF-β | Akt, PKB | phospholipase γ cleaves the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) ppp3R1/ppp3CB, calcineurin subunits | PC5A, PC5B, and PC7 | EGR1 | proprotein convertase subtilisin/kexin type 6 | substantia nigra | phosphotyrosine-interaction domain | BDNF | adaptor protein of the PDZ-LIM family | γ-aminobutyric acid, inhibitory neurotransmitter in mammalian central nervous system | Tyr | FosB/ΔFosB | IRS1/2 | LIM | dopamine transporter | enhanced green fluorescent protein | GDNF | DAT | SOS | 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine | retro-rubal field | transforming growth factor β is a secreted protein that controls proliferation and cellular differentiation | MPTP | GTPase | hypoxia-inducible factor-1alpha | GDNF family of ligands | Ret | GPI | Shank3 | NCAM | Enigma | JNK | (rearranged during transfection) canonical GDNF receptor, a receptor tyrosine kinase | PTEN | 6-OHDA | DJ-1 | (rapidly accelerated fibrosarcoma/rat fibrosarcoma) family of serine/threonine-protein kinase | SHC | NF-κB | (acronym combining the first letters of three proteins – post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) that have this common domain) protein interaction domain | phosphotyrosine-binding domains | insulin receptor substrate 1, adaptor protein, contains a PTB and PH domain | Rac1 | GFRα | nuclear factor ‘kappa-light-chain-enhancer’ of activated B-cells, transcription factor family with Rel homology domain (RHD) | catechol-O-methyltransferase | early growth response protein 1, Zif268 (zinc finger protein 225), NGFI-A (nerve growth factor-induced protein A), is a zinc finger transcription factor | serine and threonine, which can be phosphorylated | GDNF family receptor α | PKA | protein kinase A, a family of cAMP-dependent protein kinase | MAPK | NGF | SorLA | ventral tegmental area | son of sevenless, family of guanine nucleotide exchange factors that act on Ras | GABA | HIF-1a | Ras-related C3 botulinum toxin substrate 1 (Rho family), a small GTPase, like CDC42 | GAP1/2 | PTB | (Rat sarcoma) family of small membrane-associated GTPase | cycles between an active GTP-bound and an inactive GDP-bound state | glycogen synthase kinase 3β | Src | glia cell line-derived neurotrophic factor | PACE4, PCSK6 | pleckstrin homology domain | co-repressor for element-1-silencing transcription factor, a chromatin-modifying corepressor complex that acts with REST (repressor for element-1 silencing transcription factor) complex | c-Jun N-terminal kinases, members of the MAPK family of proteins | EGFP | cell division control protein 42 homolog, a plasma membrane-associated small GTPase of the Rho family | (acronym combining the first letters of three proteins – Lin11, Isl-1 and Mec-3 – that have this common domain) protein interaction domain of two contiguous zinc finger domains, separated by a two-amino acid residue hydrophobic linker | CCCP | (sarcoma protein) membrane-associated tyrosine kinase with different Src homology (SH) domains characteristic for all 9 members of the Src family kinases | DOK1/4/5/6 | (Ras homolog) family of small GTPases including Cdc42, Rac1, and RhoA | single-nucleotide polymorphism analysis | VPS10P | Rho | MEN2B | phosphatidylinositol-4,5-bisphosphate 3-kinase | 6-hydroxy-dopamine | mitogen-activated protein kinase, can phosphorylate serine, threonine, and tyrosine, e.g. p38MAPK | Cdc42 | docking proteins, have a PH and SH3 domain | GFLs | PDZ | vacuolar protein sorting 10 protein-domain receptors are type 1 transmembrane proteins | PLCγ | GTPase-activating proteins 1 and 2 | 3′,5′-cyclic adenosine monophosphate | neuronal cell adhesion molecule | TIEG | TGF-β-inducible early-response gene, a zinc finger transcription factor Vav2, adaptor protein and guanine nucleotide exchange factor for the Rho family of Ras-related GTPases | PINK1 | Raf | CoREST | multiple endocrine neoplasia 2 type B, mutation in the kinase domain of the Ret leading to constitutive active receptor | dopaminergic | glycosylphosphatidylinositol | FBJ murine osteosarcoma viral oncogene homolog B, a transcription factor with a truncated Δ form | gsk3β | ENTERIC NERVOUS-SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBSTANTIA-NIGRA | CELL BIOLOGY | MICE LACKING GDNF | C-RET | BIOPHYSICS | NEUROTROPHIC FACTOR PROMOTES | MULTIPLE ENDOCRINE NEOPLASIA | SURVIVAL IN-VIVO | RECEPTOR TYROSINE KINASE | CELL-LINE | EARLY-ONSET PARKINSONISM | Glial Cell Line-Derived Neurotrophic Factor - physiology | Parkinson Disease - pathology | Animals | Proto-Oncogene Proteins c-ret - physiology | Dopamine - physiology | Mesencephalon - metabolism | Humans | Dopaminergic Neurons - physiology | Parkinson Disease - metabolism | Synaptic Transmission | Mesencephalon - pathology | Physiological aspects | Neurons | Parkinson's disease
Rearranged during transfection | Parkinson disease | Drug addiction | Mouse model | Dopaminergic system | Glia cell line-derived neurotrophic factor | MAOA/MAOB | orphan nuclear receptor and transcription factor | cytoplasmic SH2 domain containing protein tyrosine phosphatase | Ras | RRF | COMT | PTEN-induced putative kinase 1 | SH3 and multiple ankyrin repeat domains 3, proline-rich synapse-associated protein 2 (ProSAP2) | PI3K | sorting protein-related receptor with A-type repeats, a member of the mammal Vps10p domain receptor | subunits of the Ca2+-sensitive, voltage gated A-type K+ channel | SH2 domain containing transforming protein 1 | Nurr1 | proprotein convertases | protein kinase B, serine/threonine-specific protein kinase | calcium-calmodulin-dependent protein kinase II β isoform | FRS2 | phosphatase and tensin homolog | catecholamine | SHP-2 | growth factor receptor-bound protein 2, 7 and 10, adaptor proteins | fibroblast growth factor receptor substrate 2, adaptor protein | monoamine oxidases A and B | carbonyl cyanide m-chlorophenyl hydrazone | ERK | brain derived neurotrophic factor | deglycase, oxidative stress sensor and redox-sensitive chaperone and protease | VTA | tyrosines, which can be phosphorylated | cAMP | extracellular-signal-regulated kinases, classical MAPKs | CaMKIIβ | Kv4.3 and KChip3 | GRB2/7/10 | Ser/Thr | SNP | endoplasmatic reticulum | nerve growth factor | monoamine, neurotransmitter type including dopamine, epinephrine (adrenaline) and norepinephrine (noradrenaline) | TGF-β | Akt, PKB | phospholipase γ cleaves the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) ppp3R1/ppp3CB, calcineurin subunits | PC5A, PC5B, and PC7 | EGR1 | proprotein convertase subtilisin/kexin type 6 | substantia nigra | phosphotyrosine-interaction domain | BDNF | adaptor protein of the PDZ-LIM family | γ-aminobutyric acid, inhibitory neurotransmitter in mammalian central nervous system | Tyr | FosB/ΔFosB | IRS1/2 | LIM | dopamine transporter | enhanced green fluorescent protein | GDNF | DAT | SOS | 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine | retro-rubal field | transforming growth factor β is a secreted protein that controls proliferation and cellular differentiation | MPTP | GTPase | hypoxia-inducible factor-1alpha | GDNF family of ligands | Ret | GPI | Shank3 | NCAM | Enigma | JNK | (rearranged during transfection) canonical GDNF receptor, a receptor tyrosine kinase | PTEN | 6-OHDA | DJ-1 | (rapidly accelerated fibrosarcoma/rat fibrosarcoma) family of serine/threonine-protein kinase | SHC | NF-κB | (acronym combining the first letters of three proteins – post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) that have this common domain) protein interaction domain | phosphotyrosine-binding domains | insulin receptor substrate 1, adaptor protein, contains a PTB and PH domain | Rac1 | GFRα | nuclear factor ‘kappa-light-chain-enhancer’ of activated B-cells, transcription factor family with Rel homology domain (RHD) | catechol-O-methyltransferase | early growth response protein 1, Zif268 (zinc finger protein 225), NGFI-A (nerve growth factor-induced protein A), is a zinc finger transcription factor | serine and threonine, which can be phosphorylated | GDNF family receptor α | PKA | protein kinase A, a family of cAMP-dependent protein kinase | MAPK | NGF | SorLA | ventral tegmental area | son of sevenless, family of guanine nucleotide exchange factors that act on Ras | GABA | HIF-1a | Ras-related C3 botulinum toxin substrate 1 (Rho family), a small GTPase, like CDC42 | GAP1/2 | PTB | (Rat sarcoma) family of small membrane-associated GTPase | cycles between an active GTP-bound and an inactive GDP-bound state | glycogen synthase kinase 3β | Src | glia cell line-derived neurotrophic factor | PACE4, PCSK6 | pleckstrin homology domain | co-repressor for element-1-silencing transcription factor, a chromatin-modifying corepressor complex that acts with REST (repressor for element-1 silencing transcription factor) complex | c-Jun N-terminal kinases, members of the MAPK family of proteins | EGFP | cell division control protein 42 homolog, a plasma membrane-associated small GTPase of the Rho family | (acronym combining the first letters of three proteins – Lin11, Isl-1 and Mec-3 – that have this common domain) protein interaction domain of two contiguous zinc finger domains, separated by a two-amino acid residue hydrophobic linker | CCCP | (sarcoma protein) membrane-associated tyrosine kinase with different Src homology (SH) domains characteristic for all 9 members of the Src family kinases | DOK1/4/5/6 | (Ras homolog) family of small GTPases including Cdc42, Rac1, and RhoA | single-nucleotide polymorphism analysis | VPS10P | Rho | MEN2B | phosphatidylinositol-4,5-bisphosphate 3-kinase | 6-hydroxy-dopamine | mitogen-activated protein kinase, can phosphorylate serine, threonine, and tyrosine, e.g. p38MAPK | Cdc42 | docking proteins, have a PH and SH3 domain | GFLs | PDZ | vacuolar protein sorting 10 protein-domain receptors are type 1 transmembrane proteins | PLCγ | GTPase-activating proteins 1 and 2 | 3′,5′-cyclic adenosine monophosphate | neuronal cell adhesion molecule | TIEG | TGF-β-inducible early-response gene, a zinc finger transcription factor Vav2, adaptor protein and guanine nucleotide exchange factor for the Rho family of Ras-related GTPases | PINK1 | Raf | CoREST | multiple endocrine neoplasia 2 type B, mutation in the kinase domain of the Ret leading to constitutive active receptor | dopaminergic | glycosylphosphatidylinositol | FBJ murine osteosarcoma viral oncogene homolog B, a transcription factor with a truncated Δ form | gsk3β | ENTERIC NERVOUS-SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBSTANTIA-NIGRA | CELL BIOLOGY | MICE LACKING GDNF | C-RET | BIOPHYSICS | NEUROTROPHIC FACTOR PROMOTES | MULTIPLE ENDOCRINE NEOPLASIA | SURVIVAL IN-VIVO | RECEPTOR TYROSINE KINASE | CELL-LINE | EARLY-ONSET PARKINSONISM | Glial Cell Line-Derived Neurotrophic Factor - physiology | Parkinson Disease - pathology | Animals | Proto-Oncogene Proteins c-ret - physiology | Dopamine - physiology | Mesencephalon - metabolism | Humans | Dopaminergic Neurons - physiology | Parkinson Disease - metabolism | Synaptic Transmission | Mesencephalon - pathology | Physiological aspects | Neurons | Parkinson's disease
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2003, Volume 100, Issue 5, pp. 2272 - 2277
The cytoplasmic domains (tails) of heterodimeric integrin adhesion receptors mediate integrins' biological functions by binding to cytoplasmic proteins. Most...
Proteins | Biological Sciences | Receptors | Complementary DNA | Molecular interactions | Antibodies | Ligands | CHO cells | Adhesion | Western blotting | Integrins | TYROSINE PHOSPHORYLATION | PTB DOMAIN | CELL-MIGRATION | MULTIDISCIPLINARY SCIENCES | OUTSIDE-IN | AMYLOID PRECURSOR PROTEIN | V-SRC | IDENTIFICATION | MOTIF | CHICKEN-EMBRYO FIBROBLASTS | SHC | Phosphorylation | Humans | Molecular Sequence Data | Alanine - chemistry | Cytoplasm - metabolism | Integrins - metabolism | Recombinant Fusion Proteins - metabolism | Dose-Response Relationship, Drug | Transfection | Tyrosine - chemistry | CHO Cells | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Integrin beta Chains - chemistry | Cricetinae | Mutagenesis, Site-Directed | Signal Transduction | Electrophoresis, Polyacrylamide Gel | Glutathione Transferase - metabolism | Models, Molecular | Recombinant Proteins - chemistry | DNA - metabolism | Recombinant Fusion Proteins - chemistry | Phosphotyrosine - chemistry | Precipitin Tests | Databases as Topic | Sequence Homology, Amino Acid | Animals | Protein Binding | Protein Conformation | Mice | Mutation
Proteins | Biological Sciences | Receptors | Complementary DNA | Molecular interactions | Antibodies | Ligands | CHO cells | Adhesion | Western blotting | Integrins | TYROSINE PHOSPHORYLATION | PTB DOMAIN | CELL-MIGRATION | MULTIDISCIPLINARY SCIENCES | OUTSIDE-IN | AMYLOID PRECURSOR PROTEIN | V-SRC | IDENTIFICATION | MOTIF | CHICKEN-EMBRYO FIBROBLASTS | SHC | Phosphorylation | Humans | Molecular Sequence Data | Alanine - chemistry | Cytoplasm - metabolism | Integrins - metabolism | Recombinant Fusion Proteins - metabolism | Dose-Response Relationship, Drug | Transfection | Tyrosine - chemistry | CHO Cells | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Integrin beta Chains - chemistry | Cricetinae | Mutagenesis, Site-Directed | Signal Transduction | Electrophoresis, Polyacrylamide Gel | Glutathione Transferase - metabolism | Models, Molecular | Recombinant Proteins - chemistry | DNA - metabolism | Recombinant Fusion Proteins - chemistry | Phosphotyrosine - chemistry | Precipitin Tests | Databases as Topic | Sequence Homology, Amino Acid | Animals | Protein Binding | Protein Conformation | Mice | Mutation
Journal Article
Biochemical Journal, ISSN 0264-6021, 09/2005, Volume 390, Issue 3, pp. 641 - 653
Protein-protein interactions occurring via the recognition of short peptide sequences by modular interaction domains play a central role in the assembly of...
Signal transduction | Proline-recognition domain | Src homology 3 domain (SH3 domain) | Proline-rich motif | Interaction domain | WW domain | BINDING MOTIF | PX DOMAIN | signal transduction | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIGH-AFFINITY | PHAGOCYTE NADPH OXIDASE | proline-rich motif | CRUCIAL ROLE | PROTEIN-INTERACTION NETWORKS | interaction domain | LIGAND RECOGNITION | PEPTIDE COMPLEX | proline-recognition domain | MOLECULAR-BASIS | Animals | Signal Transduction | Proline - metabolism | Protein Binding | Substrate Specificity | src Homology Domains - physiology | Evolution, Molecular | SH, Src homology | EVH1, Enabled | PEP, proline-enriched phosphatase | SH3-C, C-terminal SH3 domain | VASP (vasodilator-stimulated protein) homology | Review | Csk, C-terminal Src kinase | CD2BP2, CD2-binding protein 2 | PTB, phosphotyrosine-binding | CDR, complementarity-determining region | Fyb, Fyn-binding protein | HOG, high-osmolarity glycerol | PPII, polyproline type II | PRD, proline-recognition domain | phox, phagocyte oxidase | SLAP130, SH2-domain-containing-leucocyte-protein-of-76-kDa-associated protein | CAP, cytoskeleton-associated protein | SLP-76, SH2-domain-containing leucocyte protein of 76 kDa | PB1, phox (phagocyte oxidase) and Bem1 | SAP, signalling-lymphocytic-activation-molecule-associated protein | PX, phox homology | UEV, ubiquitin E2 variant | SLAM, signalling lymphocytic activation molecule | PH, pleckstrin homology | STAM, signal transducing adaptor molecule | MAPK, mitogen-activated protein kinase
Signal transduction | Proline-recognition domain | Src homology 3 domain (SH3 domain) | Proline-rich motif | Interaction domain | WW domain | BINDING MOTIF | PX DOMAIN | signal transduction | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIGH-AFFINITY | PHAGOCYTE NADPH OXIDASE | proline-rich motif | CRUCIAL ROLE | PROTEIN-INTERACTION NETWORKS | interaction domain | LIGAND RECOGNITION | PEPTIDE COMPLEX | proline-recognition domain | MOLECULAR-BASIS | Animals | Signal Transduction | Proline - metabolism | Protein Binding | Substrate Specificity | src Homology Domains - physiology | Evolution, Molecular | SH, Src homology | EVH1, Enabled | PEP, proline-enriched phosphatase | SH3-C, C-terminal SH3 domain | VASP (vasodilator-stimulated protein) homology | Review | Csk, C-terminal Src kinase | CD2BP2, CD2-binding protein 2 | PTB, phosphotyrosine-binding | CDR, complementarity-determining region | Fyb, Fyn-binding protein | HOG, high-osmolarity glycerol | PPII, polyproline type II | PRD, proline-recognition domain | phox, phagocyte oxidase | SLAP130, SH2-domain-containing-leucocyte-protein-of-76-kDa-associated protein | CAP, cytoskeleton-associated protein | SLP-76, SH2-domain-containing leucocyte protein of 76 kDa | PB1, phox (phagocyte oxidase) and Bem1 | SAP, signalling-lymphocytic-activation-molecule-associated protein | PX, phox homology | UEV, ubiquitin E2 variant | SLAM, signalling lymphocytic activation molecule | PH, pleckstrin homology | STAM, signal transducing adaptor molecule | MAPK, mitogen-activated protein kinase
Journal Article
Cell, ISSN 0092-8674, 2000, Volume 101, Issue 3, pp. 259 - 270
The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding...
PTB DOMAINS | F-ACTIN | EZRIN FAMILY | TERMINAL DOMAIN | PHOSPHORYLATION | INTRAMOLECULAR ASSOCIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | FAMILY MEMBERS | CELL-ADHESION | NEUROFIBROMATOSIS-2 TUMOR-SUPPRESSOR | CELL BIOLOGY | Cytoskeletal Proteins | Protein Structure, Tertiary | Amino Acid Sequence | Microfilament Proteins - chemistry | Humans | Actins - metabolism | Models, Molecular | Molecular Sequence Data | Neurofibromin 2 | Crystallography, X-Ray | Neuropeptides | Recombinant Fusion Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Protein Folding | Membrane Proteins - chemistry | Recombinant Fusion Proteins - genetics | Microfilament Proteins - metabolism | Binding Sites | Microfilament Proteins - genetics | Protein folding | Actin | Plasma membranes | Physiological aspects | Research | Cytochemistry | Binding sites (Biochemistry) | Membrane proteins
PTB DOMAINS | F-ACTIN | EZRIN FAMILY | TERMINAL DOMAIN | PHOSPHORYLATION | INTRAMOLECULAR ASSOCIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | FAMILY MEMBERS | CELL-ADHESION | NEUROFIBROMATOSIS-2 TUMOR-SUPPRESSOR | CELL BIOLOGY | Cytoskeletal Proteins | Protein Structure, Tertiary | Amino Acid Sequence | Microfilament Proteins - chemistry | Humans | Actins - metabolism | Models, Molecular | Molecular Sequence Data | Neurofibromin 2 | Crystallography, X-Ray | Neuropeptides | Recombinant Fusion Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Protein Folding | Membrane Proteins - chemistry | Recombinant Fusion Proteins - genetics | Microfilament Proteins - metabolism | Binding Sites | Microfilament Proteins - genetics | Protein folding | Actin | Plasma membranes | Physiological aspects | Research | Cytochemistry | Binding sites (Biochemistry) | Membrane proteins
Journal Article
The EMBO Journal, ISSN 0261-4189, 03/2012, Volume 31, Issue 5, pp. 1308 - 1319
Phosphotyrosine‐binding domains, typified by the SH2 (Src homology 2) and PTB domains, are critical upstream components of signal transduction pathways. The E3...
phosphotyrosine | Src substrates | ubiquitin ligases | zinc fingers | Hakai | SYSTEM | MOTIFS | UBIQUITIN LIGASE | SRC | BIOCHEMISTRY & MOLECULAR BIOLOGY | SOFTWARE | CELL BIOLOGY | SH2 DOMAIN | BREAST-CANCER | PROTEIN-RECOGNITION | ZINC-FINGERS | PTB | Protein Structure, Tertiary | Amino Acid Sequence | Cadherins - metabolism | Magnetic Resonance Spectroscopy | Protein Multimerization | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Ubiquitin-Protein Ligases - chemistry | DNA Mutational Analysis | Protein Structure, Quaternary | Protein Binding | Signal transduction | Enzymes | Eukaryotes | Amino acids | Molecular biology | Substrates | Crystal structure
phosphotyrosine | Src substrates | ubiquitin ligases | zinc fingers | Hakai | SYSTEM | MOTIFS | UBIQUITIN LIGASE | SRC | BIOCHEMISTRY & MOLECULAR BIOLOGY | SOFTWARE | CELL BIOLOGY | SH2 DOMAIN | BREAST-CANCER | PROTEIN-RECOGNITION | ZINC-FINGERS | PTB | Protein Structure, Tertiary | Amino Acid Sequence | Cadherins - metabolism | Magnetic Resonance Spectroscopy | Protein Multimerization | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Ubiquitin-Protein Ligases - chemistry | DNA Mutational Analysis | Protein Structure, Quaternary | Protein Binding | Signal transduction | Enzymes | Eukaryotes | Amino acids | Molecular biology | Substrates | Crystal structure
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2002, Volume 277, Issue 24, pp. 21749 - 21758
Cellular regulation of the ligand binding affinity of integrin adhesion receptors (integrin activation) depends on the integrin β cytoplasmic domains (tails)....
FERM DOMAIN | TYROSINE PHOSPHORYLATION | PTB DOMAIN | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID PRECURSOR PROTEIN | SURFACE-PLASMON RESONANCE | BETA-CYTOPLASMIC DOMAINS | PHORBOL ESTER | MULTIPLE SEQUENCE ALIGNMENT | CHICKEN-EMBRYO FIBROBLASTS | Surface Plasmon Resonance | Talin - chemistry | Integrins - chemistry | Molecular Sequence Data | Cytoplasm - metabolism | Flow Cytometry | Time Factors | CHO Cells | Cytoplasm - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Cricetinae | Cell Separation | Models, Molecular | Recombinant Fusion Proteins - chemistry | Cell Adhesion | Phosphotyrosine - chemistry | Protein Folding | Amino Acid Motifs | Sequence Homology, Amino Acid | Animals | Protein Binding | Ligands | Kinetics | Mutation | DNA, Complementary - metabolism
FERM DOMAIN | TYROSINE PHOSPHORYLATION | PTB DOMAIN | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID PRECURSOR PROTEIN | SURFACE-PLASMON RESONANCE | BETA-CYTOPLASMIC DOMAINS | PHORBOL ESTER | MULTIPLE SEQUENCE ALIGNMENT | CHICKEN-EMBRYO FIBROBLASTS | Surface Plasmon Resonance | Talin - chemistry | Integrins - chemistry | Molecular Sequence Data | Cytoplasm - metabolism | Flow Cytometry | Time Factors | CHO Cells | Cytoplasm - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Cricetinae | Cell Separation | Models, Molecular | Recombinant Fusion Proteins - chemistry | Cell Adhesion | Phosphotyrosine - chemistry | Protein Folding | Amino Acid Motifs | Sequence Homology, Amino Acid | Animals | Protein Binding | Ligands | Kinetics | Mutation | DNA, Complementary - metabolism
Journal Article
BMB Reports, ISSN 1976-6696, 06/2012, Volume 45, Issue 6, pp. 360 - 364
Uptake of circulating glucose into the cells happens via the insulin-mediated signalling pathway, which translocates the glucose transporter 4 (GLUT4) vesicles...
TBC1D4 (AS160) | IRAP | Isothermal titration calorimetry | Protein-protein interaction | PTB domain | PROTEIN | AS160 | MEMBRANE AMINOPEPTIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESPONSIVE AMINOPEPTIDASE | INTERACTS | SUBSTRATE | GAP
TBC1D4 (AS160) | IRAP | Isothermal titration calorimetry | Protein-protein interaction | PTB domain | PROTEIN | AS160 | MEMBRANE AMINOPEPTIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESPONSIVE AMINOPEPTIDASE | INTERACTS | SUBSTRATE | GAP
Journal Article
Cell, ISSN 0092-8674, 1999, Volume 97, Issue 4, pp. 471 - 480
The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an interaction module found in several proteins implicated in actin-based cell motility. EVH1...
LISTERIA-MONOCYTOGENES | SIGNAL-TRANSDUCTION | FOCAL ADHESION | PTB DOMAIN | PHOSPHOTYROSINE-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTIPLE ISOMORPHOUS REPLACEMENT | METABOTROPIC GLUTAMATE RECEPTORS | PROLINE-RICH MOTIF | ALDRICH-SYNDROME PROTEIN | PHOSPHOINOSITIDE BINDING | CELL BIOLOGY | Cell Adhesion Molecules - chemistry | Amino Acid Sequence | Peptides - chemistry | Humans | Actins - metabolism | Molecular Sequence Data | Structure-Activity Relationship | Phosphoproteins - metabolism | Cell Adhesion Molecules - metabolism | DNA-Binding Proteins - chemistry | Phosphoproteins - chemistry | DNA-Binding Proteins - metabolism | Sequence Homology, Amino Acid | Animals | Peptides - metabolism | Proteins - metabolism | Wiskott-Aldrich Syndrome Protein | Microfilament Proteins | Protein Conformation | Proteins - chemistry | Binding Sites | Physiological aspects | Mammals | Phosphoproteins | Actin | PEPTIDES | ACTIN | ADVANCED LIGHT SOURCE ALS | ADVANCED LIGHT SOURCE | PARTICLE ACCELERATORS | COMPLEXES
LISTERIA-MONOCYTOGENES | SIGNAL-TRANSDUCTION | FOCAL ADHESION | PTB DOMAIN | PHOSPHOTYROSINE-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTIPLE ISOMORPHOUS REPLACEMENT | METABOTROPIC GLUTAMATE RECEPTORS | PROLINE-RICH MOTIF | ALDRICH-SYNDROME PROTEIN | PHOSPHOINOSITIDE BINDING | CELL BIOLOGY | Cell Adhesion Molecules - chemistry | Amino Acid Sequence | Peptides - chemistry | Humans | Actins - metabolism | Molecular Sequence Data | Structure-Activity Relationship | Phosphoproteins - metabolism | Cell Adhesion Molecules - metabolism | DNA-Binding Proteins - chemistry | Phosphoproteins - chemistry | DNA-Binding Proteins - metabolism | Sequence Homology, Amino Acid | Animals | Peptides - metabolism | Proteins - metabolism | Wiskott-Aldrich Syndrome Protein | Microfilament Proteins | Protein Conformation | Proteins - chemistry | Binding Sites | Physiological aspects | Mammals | Phosphoproteins | Actin | PEPTIDES | ACTIN | ADVANCED LIGHT SOURCE ALS | ADVANCED LIGHT SOURCE | PARTICLE ACCELERATORS | COMPLEXES
Journal Article