ArticleMolecular and cellular biology1999
Characterization of a novel member of the DOK family that binds and modulates Abl signaling.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 102 citations in OpenAlex.
- Pan-cancer analysis identified DOK3 as a novel biomarker for predicting prognosis and immunotherapy effectiveness.Discover oncology · 2025Article
- CD200:CD200R Interactions and Their Importance in Immunoregulation.International journal of molecular sciences · 2021Review
- Emerging Roles of Downstream of Kinase 3 in Cell Signaling.Frontiers in immunology · 2020Review
- Evolutionary conservation of Ebola virus proteins predicts important functions at residue level.Bioinformatics (Oxford, England) · 2017Article
- mRNA expression of DOK1-6 in human breast cancer.World journal of clinical oncology · 2014Article
- A physical interaction between the adaptor proteins DOK3 and DAP12 is required to inhibit lipopolysaccharide signaling in macrophages.Science signaling · 2013Article
- Article
- Oncogenic tyrosine kinases target Dok-1 for ubiquitin-mediated proteasomal degradation to promote cell transformation.Molecular and cellular biology · 2011Article
- Growth-factor receptor-bound protein-2 (Grb2) signaling in B cells controls lymphoid follicle organization and germinal center reaction.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- ABL tyrosine kinases: evolution of function, regulation, and specificity.Science signaling · 2010Review
- Analysis of DOK-6 function in downstream signaling of RET in human neuroblastoma cells.Cancer science · 2010Article
- Identification of DOK genes as lung tumor suppressors.Nature genetics · 2010Article
- Dok-4 is a novel negative regulator of T cell activation.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion.The Journal of cell biology · 2009Article
- Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells.The EMBO journal · 2007Article
- 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
- Dok-R mediates attenuation of epidermal growth factor-dependent mitogen-activated protein kinase and Akt activation through processive recruitment of c-Src and Csk.Molecular and cellular biology · 2005Article
- Role of Dok-1 and Dok-2 in leukemia suppression.The Journal of experimental medicine · 2004Article
- Role of Dok-1 and Dok-2 in myeloid homeostasis and suppression of leukemia.The Journal of experimental medicine · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A novel member of the p62(dok) family of proteins, termed DOKL, is described. DOKL contains features of intracellular signaling molecules, including an N-terminal PH (pleckstrin homology) domain, a central PTB (phosphotyrosine binding) domain, and a C-terminal domain with multiple potential tyrosine phosphorylation sites and proline-rich regions, which might serve as docking sites for SH2- and SH3-containing proteins. The DOKL gene is predominantly expressed in bone marrow, spleen, and lung, although low-level expression of the RNA can also be detected in other tissues. DOKL and p62(dok) bind through their PTB domains to the Abelson tyrosine kinase in a kinase-dependent manner in both yeast and mammalian cells. DOKL is phosphorylated by the Abl tyrosine kinase in vivo. In contrast to p62(dok), DOKL lacks YxxP motifs in the C terminus and does not bind to Ras GTPase-activating protein (RasGAP) upon phosphorylation. Overexpression of DOKL, but not p62(dok), suppresses v-Abl-induced mitogen-activated protein (MAP) kinase activation but has no effect on constitutively activated Ras- and epidermal growth factor-induced MAP kinase activation. The inhibitory effect requires the PTB domain of DOKL. Finally, overexpression of DOKL in NIH 3T3 cells inhibits the transforming activity of v-Abl. These results suggest that DOKL may modulate Abl function.
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Registered trials
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