ArticleThe EMBO journal1993
The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion.
Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 204 citations in OpenAlex.
- Emerging evidence on Monkeypox: resurgence, global burden, molecular insights, genomics and possible management.Frontiers in cellular and infection microbiology · 2023Review
- p190A RhoGAP induces CDH1 expression and cooperates with E-cadherin to activate LATS kinases and suppress tumor cell growth.Oncogene · 2020Article
- p190RhoGAPs, theCells · 2019Review
- Regulation of Rho GTPase activity at the leading edge of migrating cells by p190RhoGAP.Small GTPases · 2019Review
- Cancer-associated mutations in the protrusion-targeting region of p190RhoGAP impact tumor cell migration.The Journal of cell biology · 2016Article
- p120RasGAP Protein Mediates Netrin-1 Protein-induced Cortical Axon Outgrowth and Guidance.The Journal of biological chemistry · 2016Article
- Inhibition of cell migration and invasion mediated by the TAT-RasGAP317-326 peptide requires the DLC1 tumor suppressor.Oncogene · 2014Article
- miR-142 orchestrates a network of actin cytoskeleton regulators during megakaryopoiesis.eLife · 2014Article
- RhoA is down-regulated at cell-cell contacts via p190RhoGAP-B in response to tensional homeostasis.Molecular biology of the cell · 2013Article
- Neutrophil functions and autoimmune arthritis in the absence of p190RhoGAP: generation and analysis of a novel null mutation in mice.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Gene expression profiling of monkeypox virus-infected cells reveals novel interfaces for host-virus interactions.Virology journal · 2010Article
- Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation.The Journal of biological chemistry · 2010Article
- PKCdelta influences p190 phosphorylation and activity: events independent of PKCdelta-mediated regulation of endothelial cell stress fiber and focal adhesion formation and barrier function.Biochimica et biophysica acta · 2009Article
- A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells.Journal of cell science · 2009Article
- Inactivation of Ras by p120GAP via focal adhesion kinase dephosphorylation mediates RGMa-induced growth cone collapse.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function.Molecular and cellular biology · 2003Article
- Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration.The Journal of cell biology · 2002Article
- Cytoplasmic death signal triggered by SRC-mediated phosphorylation of the adenovirus E4orf4 protein.Molecular and cellular biology · 2002Article
- Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak.The EMBO journal · 2001Article
- Downregulation of the Ras-mitogen-activated protein kinase pathway by the EphB2 receptor tyrosine kinase is required for ephrin-induced neurite retraction.Molecular and cellular biology · 2001Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Ras GTPase activating protein (GAP) possesses a C-terminal domain that interacts with GTP-bound Ras, and an N-terminal region containing two SH2 domains and an SH3 domain. In addition to its association with Ras, GAP binds stably to autophosphorylated beta PDGF receptors, and to two cytoplasmic phosphoproteins: p62, an RNA binding protein, and p190, which possesses GAP activity towards small guanine nucleotide binding proteins in the Rho/Rac family. To define the region of GAP that mediates these interactions with cellular phosphoproteins, and to investigate the biological significance of these complexes, a truncated GAP polypeptide (GAP-N) containing residues 1-445 was stably expressed in Rat-2 fibroblasts. GAP-N contains the SH2 and SH3 domains, but lacks the Ras GTPase activating domain. Stimulation of cells expressing GAP-N with PDGF induced association of GAP-N with the beta PDGF receptor, and phosphorylation of GAP-N on tyrosine, consistent with the notion that GAP SH2 domains direct binding to the autophosphorylated beta PDGF receptor in vivo. GAP-N bound constitutively to p190 in both serum-deprived and growth factor-stimulated cells. This GAP-N-p190 complex had Rho GAP activity in vitro. The expression of GAP-N in Rat-2 cells correlated with changes in the cytoskeleton and in cell adhesion, typified by the disruption of action stress fibres, a reduction in focal contacts, and an impaired ability to adhere to fibronectin. These results suggest that the N-terminal domain of GAP can direct interactions with cellular phosphoproteins in vivo, and thereby exert an effector function which modulates the cytoskeleton and cell adhesion.(ABSTRACT TRUNCATED AT 250 WORDS)
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.