ArticleCellular signalling2007
GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin.
Article in Cellular signalling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 59 citations in OpenAlex.
- CK2β Is a Gatekeeper of Focal Adhesions Regulating Cell Spreading.Frontiers in molecular biosciences · 2022Article
- Paxillin: A Hub for Mechano-Transduction from the β3 Integrin-Talin-Kindlin Axis.Frontiers in cell and developmental biology · 2022Review
- Liprin-α-Mediated Assemblies and Their Roles in Synapse Formation.Frontiers in cell and developmental biology · 2021Review
- Decreased long non-coding RNA lincFOXF1 indicates poor progression and promotes cell migration and metastasis in osteosarcoma.Journal of cellular and molecular medicine · 2020Article
- Topological features of integrin adhesion complexes revealed by multiplexed proximity biotinylation.The Journal of cell biology · 2020Article
- Proteome-level assessment of origin, prevalence and function of leucine-aspartic acid (LD) motifs.Bioinformatics (Oxford, England) · 2020Article
- Structural basis of the target-binding mode of the G protein-coupled receptor kinase-interacting protein in the regulation of focal adhesion dynamics.The Journal of biological chemistry · 2019Article
- miR-149 in Human Cancer: A Systemic Review.Journal of Cancer · 2018Review
- Functional analysis of rare variants found in schizophrenia implicates a critical role for GIT1-PAK3 signaling in neuroplasticity.Molecular psychiatry · 2017Article
- Article
- Nuclear transport of paxillin depends on focal adhesion dynamics and FAT domains.Journal of cell science · 2016Article
- Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT-PIX complexes.Journal of cell science · 2016Review
- MicroRNA-34c Suppresses Breast Cancer Migration and Invasion by Targeting GIT1.Journal of Cancer · 2016Article
- ITGA2B and ITGA8 are predictive of prognosis in clear cell renal cell carcinoma patients.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Identification of a Protein Network Driving Neuritogenesis of MGE-Derived GABAergic Interneurons.Frontiers in cellular neuroscience · 2016Article
- MiR-138 inhibits cell proliferation and reverses epithelial-mesenchymal transition in non-small cell lung cancer cells by targeting GIT1 and SEMA4C.Journal of cellular and molecular medicine · 2015Article
- Phosphorylation of tyrosine 285 of PAK1 facilitates βPIX/GIT1 binding and adhesion turnover.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Allosteric regulation of focal adhesion kinase by PIP₂ and ATP.Biophysical journal · 2015Article
- GIT1 is a novel prognostic biomarker and facilitates tumor progression via activating ERK/MMP9 signaling in hepatocellular carcinoma.OncoTargets and therapy · 2015Article
- Specific dephosphorylation at tyr-554 of git1 by ptprz promotes its association with paxillin and hic-5.PloS one · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The GIT proteins, GIT1 and GIT2, are GTPase-activating proteins for the ADP-ribosylation factor family of small GTP-binding proteins, but also serve as adaptors to link signaling proteins to distinct cellular locations. One role for GIT proteins is to link the PIX family of Rho guanine nucleotide exchange factors and their binding partners, the p21-activated protein kinases, to remodeling focal adhesions by interacting with the focal adhesion adaptor protein paxillin. We here identified the C-terminal domain of GIT1 responsible for paxillin binding. Combining structural and mutational analyses, we show that this region folds into an anti-parallel four-helix domain highly reminiscent to the focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK). Our results suggest that the GIT1 FAT-homology (FAH) domain and FAT bind the paxillin LD4 motif quite similarly. Since only a small fraction of GIT1 is bound to paxillin under normal conditions, regulation of paxillin binding was explored. Although paxillin binding to the FAT domain of FAK is regulated by tyrosine phosphorylation within this domain, we find that tyrosine phosphorylation of the FAH domain GIT1 is not involved in regulating binding to paxillin. Instead, we find that mutations within the FAH domain may alter binding to paxillin that has been phosphorylated within the LD4 motif. Thus, despite apparent structural similarity in their FAT domains, GIT1 and FAK binding to paxillin is differentially regulated.
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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.