ArticleThe EMBO journal1999
Tyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migration.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 121 citations in OpenAlex.
- Review
- Structure, Function, and Regulation of the SRMS Tyrosine Kinase.International journal of molecular sciences · 2020Review
- Nck adapter proteins promote podosome biogenesis facilitating extracellular matrix degradation and cancer invasion.Cancer medicine · 2019Article
- BRK targets Dok1 for ubiquitin-mediated proteasomal degradation to promote cell proliferation and migration.PloS one · 2014Article
- Functional dissociation between PIKfyve-synthesized PtdIns5P and PtdIns(3,5)P2 by means of the PIKfyve inhibitor YM201636.American journal of physiology. Cell physiology · 2012Article
- Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances.Frontiers in endocrinology · 2012Article
- The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes.Science signaling · 2011Article
- Characterization of DOK1, a candidate tumor suppressor gene, in epithelial ovarian cancer.Molecular oncology · 2011Article
- Oncogenic tyrosine kinases target Dok-1 for ubiquitin-mediated proteasomal degradation to promote cell transformation.Molecular and cellular biology · 2011Article
- Downstream of tyrosine kinase 1 and 2 play opposing roles in CD200 receptor signaling.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Analysis of DOK-6 function in downstream signaling of RET in human neuroblastoma cells.Cancer science · 2010Article
- Adapters in the organization of mast cell signaling.Immunological reviews · 2009Review
- The Irs1 branch of the insulin signaling cascade plays a dominant role in hepatic nutrient homeostasis.Molecular and cellular biology · 2009Article
- Nck adapter proteins: functional versatility in T cells.Cell communication and signaling : CCS · 2009Article
- Global impact of oncogenic Src on a phosphotyrosine proteome.Journal of proteome research · 2008Article
- Insulin resistance: a proinflammatory state mediated by lipid-induced signaling dysfunction and involved in atherosclerotic plaque instability.Mediators of inflammation · 2008Review
- A nuclear export signal and phosphorylation regulate Dok1 subcellular localization and functions.Molecular and cellular biology · 2006Article
- Dok-1 independently attenuates Ras/mitogen-activated protein kinase and Src/c-myc pathways to inhibit platelet-derived growth factor-induced mitogenesis.Molecular and cellular biology · 2006Article
- Irs1 and Irs2 signaling is essential for hepatic glucose homeostasis and systemic growth.The Journal of clinical investigation · 2006Article
- IkappaB kinase beta phosphorylates Dok1 serines in response to TNF, IL-1, or gamma radiation.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dok, a 62-kDa Ras GTPase-activating protein (rasGAP)-associated phosphotyrosyl protein, is thought to act as a multiple docking protein downstream of receptor or non-receptor tyrosine kinases. Cell adhesion to extracellular matrix proteins induced marked tyrosine phosphorylation of Dok. This adhesion-dependent phosphorylation of Dok was mediated, at least in part, by Src family tyrosine kinases. The maximal insulin-induced tyrosine phosphorylation of Dok required a Src family kinase. A mutant Dok (DokDeltaPH) that lacked its pleckstrin homology domain failed to undergo tyrosine phosphorylation in response to cell adhesion or insulin. Furthermore, unlike the wild-type protein, DokDeltaPH did not localize to subcellular membrane components. Insulin promoted the association of tyrosine-phosphorylated Dok with the adapter protein NCK and rasGAP. In contrast, a mutant Dok (DokY361F), in which Tyr361 was replaced by phenylalanine, failed to bind NCK but partially retained the ability to bind rasGAP in response to insulin. Overexpression of wild-type Dok, but not that of DokDeltaPH or DokY361F, enhanced the cell migratory response to insulin without affecting insulin activation of mitogen-activated protein kinase. These results identify Dok as a signal transducer that potentially links, through its interaction with NCK or rasGAP, cell adhesion and insulin receptors to the machinery that controls cell motility.
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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.