ArticleMolecular biology of the cell2002
Distinct recruitment and function of Gab1 and Gab2 in Met receptor-mediated epithelial morphogenesis.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 59 citations in OpenAlex.
- AberrantCells · 2024Review
- The Role of GAB1 in Cancer.Cancers · 2023Review
- HGF/c-Met: A Key Promoter in Liver Regeneration.Frontiers in pharmacology · 2022Review
- Increased levels of Gab1 and Gab2 adaptor proteins skew interleukin-4 (IL-4) signaling toward M2 macrophage-driven pulmonary fibrosis in mice.The Journal of biological chemistry · 2017Article
- Extracellular Signal-Regulated Kinases 1 and 2 Phosphorylate Gab2 To Promote a Negative-Feedback Loop That Attenuates Phosphoinositide 3-Kinase/Akt Signaling.Molecular and cellular biology · 2017Article
- Cleavage of Grb2-Associated Binding Protein 2 by Viral Proteinase 2A duringFrontiers in cellular and infection microbiology · 2017Article
- Novel role for p21-activated kinase 2 in thrombin-induced monocyte migration.The Journal of biological chemistry · 2013Article
- GAB2 induces tumor angiogenesis in NRAS-driven melanoma.Oncogene · 2013Article
- Alterations of Gab2 signalling complexes in imatinib and dasatinib treated chronic myeloid leukaemia cells.Cell communication and signaling : CCS · 2013Article
- Gab2 phosphorylation by RSK inhibits Shp2 recruitment and cell motility.Molecular and cellular biology · 2013Article
- Gab docking proteins in cardiovascular disease, cancer, and inflammation.International journal of inflammation · 2013Article
- Anti-apoptotic role of caspase-cleaved GAB1 adaptor protein in hepatocyte growth factor/scatter factor-MET receptor protein signaling.The Journal of biological chemistry · 2012Article
- Participation of Gab1 and Gab2 in IL-22-mediated keratinocyte proliferation, migration, and differentiation.Molecular and cellular biochemistry · 2012Article
- Met receptor tyrosine kinase signals through a cortactin-Gab1 scaffold complex, to mediate invadopodia.Journal of cell science · 2012Article
- Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal transduction by the related receptor tyrosine kinases RON and MET.The Journal of biological chemistry · 2011Article
- The role of the c-Met pathway in lung cancer and the potential for targeted therapy.Therapeutic advances in medical oncology · 2011Article
- GGA3 functions as a switch to promote Met receptor recycling, essential for sustained ERK and cell migration.Developmental cell · 2011Article
- c-Jun N-terminal Kinase 2 Regulates Multiple Receptor Tyrosine Kinase Pathways in Mouse Mammary Tumor Growth and Metastasis.Genes & cancer · 2011Article
- Function, regulation and pathological roles of the Gab/DOS docking proteins.Cell communication and signaling : CCS · 2009Article
- Pak4, a novel Gab1 binding partner, modulates cell migration and invasion by the Met receptor.Molecular and cellular biology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gab family of docking proteins (Gab1 and Gab2) are phosphorylated in response to various cytokines and growth factors. Gab1 acts to diversify the signal downstream from the Met receptor tyrosine kinase through the recruitment of multiple signaling proteins, and is essential for epithelial morphogenesis. To determine whether Gab1 and Gab2 are functionally redundant, we have examined the role of Gab2 in epithelial cells. Both Gab1 and Gab2 are expressed in epithelial cells and localize to cell-cell junctions. However, whereas overexpression of Gab1 promotes a morphogenic response, the overexpression of Gab2 fails to induce this response. We show that Gab2 recruitment to the Met receptor is dependent on the Grb2 adapter protein. In contrast, Gab1 recruitment to Met is both Grb2 dependent and Grb2 independent. The latter requires a novel amino acid sequence present in the Met-binding domain of Gab1 but not Gab2. Mutation of these residues in Gab1 impairs both association with the Met receptor and the ability of Gab1 to promote a morphogenic response, whereas their insertion into Gab2 increases Gab2 association with Met, but does not confer on Gab2 the ability to promote epithelial morphogenesis. We propose that the Grb2-independent recruitment of Gab proteins to Met is necessary but not sufficient to promote epithelial morphogenesis.
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Registered trials
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.