ArticleMolecular and cellular biology2001
Inhibition of the motility and growth of B16F10 mouse melanoma cells by dominant negative mutants of Dok-1.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Nck adapter proteins promote podosome biogenesis facilitating extracellular matrix degradation and cancer invasion.Cancer medicine · 2019Article
- Subcellular compartmentalization of docking protein-1 contributes to progression in colorectal cancer.EBioMedicine · 2016Article
- BRK targets Dok1 for ubiquitin-mediated proteasomal degradation to promote cell proliferation and migration.PloS one · 2014Article
- Transcriptional regulation of the human tumor suppressor DOK1 by E2F1.Molecular and cellular biology · 2012Article
- Characterization of DOK1, a candidate tumor suppressor gene, in epithelial ovarian cancer.Molecular oncology · 2011Article
- CAV1 inhibits metastatic potential in melanomas through suppression of the integrin/Src/FAK signaling pathway.Cancer research · 2010Article
- Advances in targeting IKK and IKK-related kinases for cancer therapy.Clinical cancer research : an official journal of the American Association for Cancer Research · 2008Review
- Chemical groups that adhere to the surfaces of living malignant cells.Pharmaceutical research · 2007Article
- Atomic force microscopy study of the specific adhesion between a colloid particle and a living melanoma cell: Effect of the charge and the hydrophobicity of the particle surface.Biophysical journal · 2006Article
- A nuclear export signal and phosphorylation regulate Dok1 subcellular localization and functions.Molecular and cellular biology · 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
- c-Abl phosphorylates Dok1 to promote filopodia during cell spreading.The Journal of cell biology · 2004Article
- Article
- A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function.Molecular and cellular biology · 2003Article
- Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites.The Journal of cell biology · 2002Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dok-1 (p62(Dok)) is a multiple-site docking protein that acts downstream of receptor and nonreceptor tyrosine kinases. Although it has been proposed to contribute to the control of cell growth and migration through association with the Ras GTPase-activating protein and the adapter protein Nck, the role of Dok-1 remains largely unknown. The functions of Dok-1 have now been investigated by the generation of two different COOH-terminal truncation mutants of this protein: one (DokPH+PTB) containing the pleckstrin homology and phosphotyrosine-binding domains, and the other (DokPH) composed only of the pleckstrin homology domain. Both of these mutant proteins were shown to act in a dominant negative manner. Overexpression of each of the mutants in highly metastatic B16F10 mouse melanoma cells thus both inhibited the tyrosine phosphorylation of endogenous Dok-1 induced by cell adhesion as well as reduced the association of the endogenous protein with cellular membranes and the cytoskeleton. Overexpression of DokPH+PTB in these cells also markedly reduced both the rates of cell spreading, migration, and growth as well as the extent of Ras activation. The effects of DokPH on these processes were less pronounced than were those of DokPH+PTB, indicating the importance of the phosphotyrosine-binding domain. These results suggest that at least in B16F10 cells, Dok-1 positively regulates not only cell spreading and migration but also cell growth and Ras activity.
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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.