Affinage

DOK1

Docking protein 1 · UniProt Q99704

Length
481 aa
Mass
52.4 kDa
Annotated
2026-06-09
91 papers in source corpus 41 papers cited in narrative 40 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DOK1 (p62dok) is a multi-domain docking protein that acts predominantly as a negative regulator of Ras/ERK/MAPK and PI3K/Akt signaling downstream of growth factor, cytokine, integrin, and immune receptors (PMID:11489947, PMID:11489946, PMID:15611294, PMID:15611295). Following PI3-kinase activation, DOK1 is recruited to the plasma membrane through its PH domain binding 3'-phosphoinositides (including PtdIns5P), a step essential for both its tyrosine phosphorylation and its inhibitory output (PMID:11489946, PMID:11825908, PMID:19299694). Once membrane-localized, DOK1 is phosphorylated on C-terminal tyrosines by an array of kinases—Bcr-Abl, c-Abl, Src/Lyn, the insulin receptor, RET, and others—creating docking sites that recruit p120 RasGAP (whose tandem SH2 domains engage doubly phosphorylated DOK1 to spatially localize Ras inhibition rather than alter GAP catalysis), and the Nck adaptor via Y361 (PMID:9008160, PMID:10688886, PMID:11551902, PMID:12087092, PMID:37507023). Its PTB domain binds phosphotyrosine NPXY motifs—structurally defined in complex with a RET phosphopeptide—and recruits SHIP1, SHP-1, and the phospho-Y747 β3 integrin tail in competition with talin, the latter constituting a phosphotyrosine switch that governs integrin outside-in signaling (PMID:11042170, PMID:14607833, PMID:18156175, PMID:10822173, PMID:10585470). Through these activities DOK1 restrains cell proliferation while promoting cell spreading, migration, and filopodia formation via c-Abl–dependent Y361–Nck recruitment (PMID:15148308, PMID:16537894, PMID:16705178). DOK1 and the paralog DOK2 cooperatively suppress myeloproliferation, and loss of both produces CML-like disease, while oncogenic tyrosine kinases inactivate DOK1 via ubiquitin-proteasome–dependent degradation (PMID:15611294, PMID:15611295, PMID:21536658). DOK1 additionally serine-phosphorylated by IKKbeta couples inflammatory signaling to its regulatory function, shuttles between nucleus and cytoplasm under CRM1 control, and serves as a negative feedback brake across B, T, NK, mast, and macrophage immune responses (PMID:15574499, PMID:15699069, PMID:16705178, PMID:17329234, PMID:24963146, PMID:35421591).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1997 High

    Establishing DOK1 as a constitutively phosphorylated RasGAP-associated protein in leukemic cells defined it as a candidate node linking aberrant tyrosine kinase activity to Ras pathway control.

    Evidence Biochemical purification and co-IP from CML progenitor cells and c-Kit-activated hematopoietic lines

    PMID:9008160

    Open questions at the time
    • Did not establish whether the RasGAP association was functionally inhibitory or activating
    • No domain mapping of the interaction
  2. 2000 High

    Demonstrating that Bcr-Abl directly phosphorylates DOK1 C-terminal tyrosines required for RasGAP binding, and that phospho-DOK1 inhibits RasGAP activity, gave the first direct mechanism for DOK1-mediated Ras regulation.

    Evidence In vitro kinase assay with recombinant p210(bcr-abl), site-directed mutagenesis, RasGAP activity assay

    PMID:10688886

    Open questions at the time
    • In vitro RasGAP inhibition not directly tied to cellular Ras output
    • Identity of additional cooperating effectors unknown
  3. 2000 High

    Genetic knockout and chimeric receptor reconstitution placed DOK1 as the negative regulatory module of FcgammaRIIB/BCR signaling, showing its structural information alone is sufficient to inhibit ERK.

    Evidence DOK1 knockout by homologous recombination, Lyn-dependent phosphorylation assays, chimeric FcgammaRIIB reconstitution, proliferation assays in B cells

    PMID:10640270 PMID:10755621 PMID:10822173

    Open questions at the time
    • Mechanism downstream of RasGAP recruitment in B cells incompletely defined
    • SHIP1-DOK1 vs RasGAP-DOK1 complex switching not resolved spatially
  4. 2001 High

    Knockout mouse models and PI3K/PH-domain dissection established DOK1 as a physiological negative regulator of growth factor–induced Ras/MAPK signaling whose membrane recruitment, not solely RasGAP/Nck binding, drives inhibition and opposes leukemogenesis.

    Evidence p62(dok)-/- mice, retroviral bone marrow transplantation, PI3K inhibition with PH-domain mutants, membrane fractionation, insulin receptor in vitro kinase assays

    PMID:11489946 PMID:11489947 PMID:11551902 PMID:11825908

    Open questions at the time
    • The RasGAP/Nck-independent inhibitory effector remained unidentified
    • Single-knockout phenotype mild, hinting at redundancy
  5. 2002 High

    Mapping DOK1's interactions with RET and activin receptors separated RasGAP-dependent ERK suppression from Nck-dependent JNK activation and revealed a phosphorylation-independent adaptor role linking TGF-beta family receptors to Smad3.

    Evidence Yeast two-hybrid, gene-trap screening, mutagenesis, co-IP, Ras/Erk, JNK and apoptosis assays

    PMID:11927552 PMID:12087092

    Open questions at the time
    • Smad3 linkage based on single-lab co-IP
    • Physiological contribution of DOK1 to activin signaling in vivo untested
  6. 2003 High

    The crystal structure of the DOK1 PTB domain bound to a RET phosphopeptide provided the atomic basis for its phosphotyrosine recognition and selectivity against Shc/IRS1 ligands.

    Evidence X-ray crystallography of PTB domain alone and in complex, peptide binding assays

    PMID:14607833

    Open questions at the time
    • No structure of full-length DOK1 or PH domain
    • Did not capture EGFR or integrin tail complexes
  7. 2004 High

    c-Abl-dependent Y361 phosphorylation and Nck recruitment were shown to drive filopodia formation, establishing a positive cytoskeletal role for DOK1 distinct from its inhibitory signaling functions.

    Evidence c-Abl-/-, Dok1-/-, Nck-/- fibroblasts with rescue, immunofluorescence, co-IP

    PMID:15148308

    Open questions at the time
    • Downstream actin regulators of the Nck arm not defined
    • Reconciliation of pro-migratory and anti-proliferative roles not addressed
  8. 2004 High

    Double-knockout mice and IKKbeta serine phosphorylation studies revealed DOK1/DOK2 redundancy in suppressing myeloproliferation and a serine-phosphorylation input coupling inflammatory kinases to DOK1 function.

    Evidence Dok1/Dok2 single and double knockout mice, in vitro IKKbeta kinase assay, S-to-A/S-to-E mutagenesis, ERK/motility assays

    PMID:15574499 PMID:15611294 PMID:15611295

    Open questions at the time
    • How serine phosphorylation mechanistically alters DOK1 activity unresolved
    • Division of labor between DOK1 and DOK2 not fully mapped
  9. 2004 Medium

    Systematic mutagenesis showed that Y336/Y340 are required for Ras-Erk inhibition independently of RasGAP binding, formalizing the existence of an unidentified cooperating effector.

    Evidence C-terminal deletion and point mutants, Erk and v-Abl transformation assays

    PMID:15189452

    Open questions at the time
    • The cooperating Y336/Y340-recruited molecule was never identified
    • Single-lab mutagenesis without biochemical isolation of the partner
  10. 2005 High

    Knockout-plus-Y/F-mutant reconstitution defined DOK1/DOK2 as tyrosine-phosphorylation-dependent brakes on TLR4/ERK signaling and inflammatory cytokine output in macrophages.

    Evidence Knockout macrophages, Y/F mutant reconstitution, ERK/NF-kappaB assays, cytokine measurement, in vivo LPS challenge

    PMID:15699069

    Open questions at the time
    • Kinase responsible for TLR4-induced DOK1 phosphorylation not pinned down
    • Selectivity for ERK over other MAPKs mechanistically unexplained
  11. 2006 High

    Pathway dissection revealed DOK1 inhibits mitogenesis through two arms—Csk recruitment to Src attenuating c-myc, and RasGAP plus an additional effector—and demonstrated CRM1-dependent nucleocytoplasmic shuttling tied to its anti-proliferative and pro-spreading functions.

    Evidence Knockout cells with binding-deficient mutants, Csk co-IP, c-myc/Src assays, leptomycin B treatment, NES mutagenesis, localization and functional assays

    PMID:16537894 PMID:16705178

    Open questions at the time
    • Nuclear function of DOK1, if any, undefined
    • The additional RasGAP-cooperating effector still unidentified
  12. 2007 High

    Structural and genetic studies established the beta3 integrin Y747 phosphotyrosine switch between talin and DOK1 PTB binding, and defined DOK1/DOK2 as negative regulators of TCR/ZAP-70 signaling via a C-terminal-motif-independent mechanism.

    Evidence NMR and X-ray with affinity quantification of beta3 tail; double-knockout mice and forced expression in T cells with truncation mutants

    PMID:17329234 PMID:18156175

    Open questions at the time
    • The C-terminal-independent mechanism inhibiting ZAP-70 not identified
    • Cellular trigger for beta3 Y747 phosphorylation not defined
  13. 2008 High

    Genetic epistasis through PPARgamma-S112A rescue established a DOK1-ERK-PPARgamma axis controlling adipocyte hypertrophy, extending DOK1's ERK-suppressive role to metabolic physiology.

    Evidence Dok1-knockout adipocytes and MEFs, PPARgamma S112 phosphorylation assay, PPARgamma-S112A genetic rescue in mice

    PMID:18204460

    Open questions at the time
    • Direct molecular link from DOK1 to the relevant ERK pool in adipocytes not shown
    • Whether the same axis operates in human adipose tissue untested
  14. 2009 Medium

    Identification of PtdIns5P as a PH-domain ligand connected lipid second-messenger production to DOK1 tyrosine phosphorylation and negative function in T cells.

    Evidence In vitro lipid binding, intracellular PtdIns5P modulation, PH-deletion mutants, phosphorylation assays in T cells

    PMID:19299694

    Open questions at the time
    • Single-lab lipid binding without structural validation of the PH-PtdIns5P interaction
    • Relative contributions of PtdIns5P versus PI3K products unclear
  15. 2011 Medium

    Demonstration that oncogenic Bcr-Abl and Src target DOK1 for ubiquitin-proteasome degradation showed that tumor kinases inactivate DOK1 by destruction, and that degradation-resistant DOK1 more strongly suppresses transformation.

    Evidence Proteasome inhibition, ubiquitination assay, degradation-resistant mutant, transformation assay

    PMID:21536658

    Open questions at the time
    • E3 ligase responsible not identified
    • Single-lab study without in vivo confirmation
  16. 2014 Medium

    Studies of BRK and PDGF-BB/glioma signaling refined DOK1 as both a degradation substrate of pro-tumorigenic kinases and a Y362/Y398-dependent driver of p130Cas/Rap1-mediated invasion.

    Evidence Co-IP, in vitro kinase and ubiquitination assays, phosphosite mutants, Rap1 activation and 3D invasion assays

    PMID:24523872 PMID:24762811

    Open questions at the time
    • Reconciliation of DOK1's tumor-suppressive versus pro-invasive roles unresolved
    • Both findings rest on single-lab knockdown/overexpression systems
  17. 2016 High

    A clean platelet knockout established DOK1 as a selective negative regulator of integrin alphaIIbbeta3 outside-in (not inside-out) signaling, with in vivo consequences for thrombosis and bleeding.

    Evidence Dok-1-/- mice, platelet clot retraction/spreading assays, PLCgamma2 phosphorylation, in vivo carotid thrombosis model

    PMID:26790499

    Open questions at the time
    • Molecular basis for outside-in selectivity not resolved
    • Direct competition with talin in platelets not demonstrated in this system
  18. 2023 Medium

    Biophysical analysis of the RasGAP-DOK1 interface showed dual SH2 engagement confers ~100-fold selectivity without altering GAP catalysis, reframing RasGAP recruitment as spatial localization rather than direct enzymatic modulation.

    Evidence Affinity measurements, small-angle X-ray scattering, in vitro RasGAP activity assay

    PMID:37507023

    Open questions at the time
    • No cell-based validation of the localization model
    • Apparent tension with earlier in vitro RasGAP-inhibition reports unreconciled

Open questions

Synthesis pass · forward-looking unresolved questions
  • The identity of the RasGAP-independent effector recruited via Y336/Y340 that cooperates to inhibit Ras-Erk signaling, and the unifying mechanism reconciling DOK1's anti-proliferative versus pro-migratory/pro-invasive roles, remain unresolved.
  • No biochemical isolation of the Y336/Y340-binding partner
  • No single framework linking DOK1's tumor-suppressive and pro-invasive activities
  • Context determinants selecting RasGAP versus Nck versus SHIP1 complexes undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0098772 molecular function regulator activity 4 GO:0008092 cytoskeletal protein binding 2 GO:0008289 lipid binding 2
Localization
GO:0005886 plasma membrane 4 GO:0005634 nucleus 2 GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1643685 Disease 4 R-HSA-168256 Immune System 4 R-HSA-109582 Hemostasis 1
Partners
CSKINPP5DITGB3NCK1PTPN6RASA1SH2D1AYWHAZ

Evidence

Reading pass · 40 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 p62(dok)/DOK1 is a constitutively tyrosine-phosphorylated protein in CML progenitor cells that associates with the p120 RasGTPase-activating protein (RasGAP); association with RasGAP correlates with its tyrosine phosphorylation. DOK1 is also rapidly tyrosine-phosphorylated upon activation of the c-Kit receptor tyrosine kinase. Biochemical purification, co-immunoprecipitation, SDS-PAGE/Western blot from CML progenitor cells and hematopoietic cell lines Cell High 9008160
2000 Tyrosine-phosphorylated p62(dok) directly inhibits RasGAP activity in vitro. p210(bcr-abl) directly phosphorylates p62(dok) on C-terminal tyrosine residues, and this phosphorylation is required for RasGAP binding. Five C-terminal tyrosines are involved in RasGAP binding in vitro. In vitro kinase assay with recombinant p210(bcr-abl), site-directed mutagenesis, RasGAP activity assay Proceedings of the National Academy of Sciences of the United States of America High 10688886
1999 Cell adhesion to extracellular matrix induces tyrosine phosphorylation of DOK1 via Src family kinases; the pleckstrin homology (PH) domain is required for membrane localization and adhesion-dependent phosphorylation. Insulin promotes DOK1 association with NCK (via Y361) and RasGAP, and overexpression of wild-type DOK1 (but not PH-domain or Y361F mutants) enhances insulin-stimulated cell migration. Site-directed mutagenesis (DeltaPH, Y361F), co-immunoprecipitation, cell migration assay, subcellular fractionation/localization The EMBO journal High 10202139
2000 DOK1 functions as a negative regulator of BCR-mediated MAP kinase signaling in B cells; upon BCR or BCR/FcgammaRIIB co-crosslinking, DOK1 is tyrosine phosphorylated in a Lyn-dependent manner. DOK1 knockout (homologous recombination) results in increased ERK activation and abolishes FcgammaRIIB-mediated negative regulation of cell proliferation. Gene knockout by homologous recombination, Western blot for phosphorylation, cell proliferation assay, genetic epistasis Genes & development High 10640270
2000 FcgammaRIIB-BCR co-aggregation leads to increased tyrosine phosphorylation of DOK1 and increased RasGAP binding. SHIP (phosphatidylinositol 5-phosphatase) recruits DOK1 via DOK1's PTB domain after being recruited and phosphorylated by FcgammaRIIB. A chimeric FcgammaRIIB containing the RasGAP-binding domain of DOK1 mediates FcgammaRIIB inhibition of ERK activation, demonstrating DOK1's structural information is sufficient for this inhibitory effect. Co-immunoprecipitation, chimeric receptor reconstitution, signaling assays in B cells Immunity High 10755621
2000 DOK1 is a major tyrosine-phosphorylated protein in v-Src-transformed cells; the PTB domain and C-terminal tail (residues 336-363) of DOK1 are both necessary for inhibition of Src-mediated cellular transformation. The PTB domain binds phosphopeptides with consensus motif Y/MXXNXL-pY. DOK1 homodimerizes through its PTB domain and Y146; mutations blocking homodimerization reduce DOK1's ability to inhibit Src transformation. Combinatorial peptide library, site-directed mutagenesis, cellular transformation assay, co-immunoprecipitation The Journal of biological chemistry High 11042170
2001 Loss of p62(dok) in knockout mice results in increased cell proliferation and sustained Ras/MAPK activation after growth factor removal; p62(dok) acts as a negative regulator of growth factor-induced Ras/MAPK signaling and opposes p210(bcr-abl)-induced leukemogenesis by shortening latency of myeloproliferative disease. p62(dok)-/- mouse model, proliferation assay, Ras/MAPK activation assay, retroviral bone marrow transduction/transplantation The Journal of experimental medicine High 11489947
2001 PI3-kinase-dependent membrane recruitment of p62(dok) via its PH domain binding 3'-phosphorylated phosphoinositides is essential for its negative effect on PDGFR/Ras/MAPK signaling; p62(dok) can exert its negative effect on the MAPK pathway independently of its ability to associate with RasGAP and Nck. p62(dok)-/- cell reconstitution, PI3-kinase inhibition, PH domain mutants, membrane fractionation, MAPK assay The Journal of experimental medicine High 11489946
2001 Insulin receptor (IR) directly phosphorylates p62(dok) at Y362 and Y398 in vitro; Y362 phosphorylation is required for Nck binding and Y362/Y398 phosphorylation are required for RasGAP binding. Mutations at Y362/Y398 decrease inhibitory effect of p62(dok) on insulin-stimulated Ras and Akt activation. DOK1 inhibitory effect on Akt is upstream of Ras (blocked by constitutively active Ras). In vitro kinase assay, site-directed mutagenesis (Y362F, Y398F), co-immunoprecipitation, Ras and Akt activation assays The Journal of biological chemistry High 11551902
2002 DOK1 binds RET receptor tyrosine kinase (identified by yeast two-hybrid); Y361 of Dok1 is the binding site for Nck; Y295, Y314, Y361, Y376, Y397, and Y408 mediate RasGAP binding. Overexpression of Dok1 or Y361F mutant suppresses RET-induced Ras/Erk activation (RasGAP-dependent), while Nck binding to Y361 is required for JNK/c-Jun activation by RET. Yeast two-hybrid, site-directed mutagenesis, co-immunoprecipitation, Ras/Erk and JNK activation assays The Journal of biological chemistry High 12087092
2002 DOK1 acts as an adaptor that links activin (TGF-beta family) receptors with Smad3 and Smad4 in a tyrosine phosphorylation-independent manner. Activin stimulation triggers DOK1 association with Smad3 and association of Smad3 with Smad4. DOK1 is associated with both type I and type II activin receptors. Overexpression of DOK1 augments activin A-induced apoptosis and down-regulates bcl-XL via inhibition of the Ras/Erk pathway. Retroviral gene trap screening, co-immunoprecipitation, apoptosis assay, Western blot The EMBO journal Medium 11927552
2002 DOK1 associates with the juxtamembrane region and C-terminal tail of c-Kit; PI3-kinase activation by c-Kit ligand promotes DOK1 PH domain binding and membrane recruitment; Lyn is required for KL-dependent DOK1 tyrosine phosphorylation (demonstrated using Lyn-deficient bone marrow mast cells); both Lyn and Tec can phosphorylate DOK1 in vitro. Membrane localization is required for DOK1's function as a negative regulator of cell proliferation. PI3-kinase inhibition, constitutively membrane-targeted DOK1 mutant, Lyn-deficient primary cells, in vitro kinase assay, membrane fractionation, proliferation assay The Journal of biological chemistry High 11825908
2003 Crystal structure of the Dok1 PTB domain alone and in complex with a phosphopeptide derived from RET receptor tyrosine kinase was solved. The PTB domain consists of a beta-sandwich of two antiparallel beta-sheets capped by a C-terminal alpha-helix; the RET phosphopeptide binds in a surface groove between strand beta5 and the C-terminal alpha-helix. Dok1 PTB does not recognize peptide sequences from TrkA or IL-4 (recognized by Shc and IRS1). X-ray crystallography, peptide binding assay The Journal of biological chemistry High 14607833
2004 c-Abl tyrosine kinase phosphorylates DOK1 at Y361 during cell spreading, promoting DOK1 association with the Nck SH2/SH3 adaptor. Each component (c-Abl, DOK1, Nck) is required for filopodia formation during cell spreading; cells lacking c-Abl, DOK1, or Nck have fewer filopodia. DOK1 and c-Abl act in the same signaling pathway and are both detected in filopodia of spreading cells. Genetic knockout fibroblasts (c-Abl-/-, Dok1-/-, Nck-/-), rescue by re-expression, specific substrate identification assay, immunofluorescence/localization, co-immunoprecipitation The Journal of cell biology High 15148308
2004 Dok1 and Dok2 double-deficient mice spontaneously develop CML-like myeloproliferative disease; myeloid cells show hyperproliferation and hypo-apoptosis, with enhanced Erk and Akt activation upon cytokine stimulation. Single knockouts show normal steady-state hematopoiesis, establishing cooperative/redundant roles. Single and double knockout mouse generation, hematopoiesis analysis, proliferation/apoptosis assay, Erk/Akt signaling assay, bone marrow transplantation The Journal of experimental medicine High 15611294 15611295
2004 IKKbeta associates with and phosphorylates DOK1 at S439, S443, S446, and S450 in response to TNF-alpha, IL-1, or gamma radiation. Recombinant IKKbeta phosphorylates DOK1 in vitro. DOK1 with serine-to-alanine mutations at these sites fails to inhibit PDGF-induced ERK activation or cell growth, and also fails to promote cell motility. Serine-phosphorylation-mimicking mutant (EEEE) further enhances cell motility. In vitro kinase assay with recombinant IKKbeta, site-directed mutagenesis (S-to-A and S-to-E), phospho-site-specific antisera, ERK assay, cell growth and motility assay Proceedings of the National Academy of Sciences of the United States of America High 15574499
2004 DOK1 tyrosine residues Y336 and Y340 are essential for the negative regulation of Ras-Erk signaling but dispensable for RasGAP binding, indicating DOK1 recruits an additional, unidentified molecule that cooperates with RasGAP to inhibit Ras-Erk signaling and cellular transformation. C-terminal deletion mutants, site-directed mutagenesis (Y336F, Y340F, Y295F, Y361F), Erk activation assay, v-Abl transformation assay Genes to cells Medium 15189452
2004 DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin beta3 subunit in response to IGF-I in vascular smooth muscle cells. IGF-I induces DOK1 binding to beta3 and to SHP-2; blocking DOK1/beta3 or DOK1/SHP-2 interactions (with synthetic peptides or non-binding DOK1 mutant) inhibits SHP-2 recruitment to beta3 and impairs IGF-I-dependent Akt and MAPK phosphorylation, cell migration and proliferation. Co-immunoprecipitation, synthetic peptide blocking, DOK1 mutant expression, Akt/MAPK assays, cell migration/proliferation assays The Journal of biological chemistry Medium 15546884
2004 Only the Dok1 PTB domain (not Dok4 or Dok5) specifically binds to phosphorylated Y1086 and Y1148 in EGFR, as shown by yeast two-hybrid and biochemical binding assays; structure-based mutagenesis defines molecular determinants for two distinct Dok1 PTB domain/EGFR interactions. Yeast two-hybrid, biochemical binding assays, structure-based mutagenesis Journal of molecular biology Medium 15476828
2005 LPS (via TLR4) rapidly induces tyrosine phosphorylation of DOK1 and Dok2 in macrophages. Macrophages lacking DOK1 or Dok2 show elevated Erk activation (but not NF-kappaB or other MAPKs) and hyperproduction of TNF-alpha and nitric oxide. A Tyr/Phe substitution mutant of DOK1 fails to inhibit LPS-induced Erk activation, establishing tyrosine phosphorylation as mechanistically required. Macrophages respond normally to TLR agonists that do not induce DOK1 tyrosine phosphorylation. Knockout macrophages, forced expression with Y/F mutant, Erk/NF-kappaB signaling assays, cytokine measurements, in vivo LPS challenge The Journal of experimental medicine High 15699069
2006 DOK1 inhibits PDGF-stimulated mitogenesis by two independent pathways: (1) recruiting Csk to active Src kinases (via a specific domain), thereby attenuating c-myc induction; and (2) negatively regulating Ras/MAPK activation via RasGAP and at least one additional DOK1-interacting protein. Both pathways contribute to DOK1's inhibitory effect on mitogenesis. DOK1 knockout cells, DOK1 interaction-deficient mutants, c-myc induction assay, Src activity assay, Csk co-IP, Ras/MAPK assay, proliferation assay Molecular and cellular biology High 16537894
2006 DOK1 shuttles between the nucleus and cytoplasm; a functional nuclear export signal (NES: 348LLKAKLTDPKED359) keeps DOK1 cytoplasmic. CRM1 inhibition (leptomycin B) causes nuclear accumulation. Src-induced tyrosine phosphorylation and IKKbeta both promote cytoplasmic localization. Serum starvation or cell suspension favors nuclear localization; serum/growth factor/adhesion promotes cytoplasmic localization. Nuclear NES-mutant DOK1 has impaired ability to inhibit cell proliferation, promote cell spreading and cell motility. Leptomycin B treatment, NES mutagenesis, subcellular fractionation, live-cell imaging, proliferation/spreading/migration assays Molecular and cellular biology High 16705178
2007 NMR spectroscopy and X-ray crystallography show that phosphorylation of Y747 in the beta3 integrin tail acts as a switch: unphosphorylated beta3 tail binds talin more strongly than DOK1 PTB domain; upon Y747 phosphorylation, DOK1 PTB domain binds much more strongly than talin. DOK1 interacts exclusively with the canonical NPXY motif of beta3, unlike talin. NMR (15N-1H HSQC titrations, chemical shift mapping), X-ray crystallography, affinity quantification The Journal of biological chemistry High 18156175
2007 Dok-1 and Dok-2 negatively regulate TCR signaling; mice lacking both show augmented responses to thymus-dependent antigens and elevated ZAP-70 activation. Forced expression of Dok-1 or Dok-2 in CD3+CD4+ T cell clone inhibits ZAP-70 activation. The C-terminal SH2-target motifs are dispensable for this negative regulation, indicating a distinct, unidentified mechanism. Double knockout mice, forced expression in T cell clone, ZAP-70 phosphorylation assay, proliferation/cytokine assays, C-terminal truncation mutants International immunology High 17329234
2008 DOK1 promotes adipocyte hypertrophy by counteracting the inhibitory effect of ERK on PPARgamma. In Dok1-deficient embryonic fibroblasts, ERK activity is elevated, leading to increased phosphorylation of PPARgamma on S112 (a negative regulatory site for PPARgamma transactivation). Mutation of PPARgamma S112 blocks the lean phenotype caused by Dok1 ablation in mice, establishing the DOK1-ERK-PPARgamma axis. Dok1-knockout mouse adipocytes and embryonic fibroblasts, PPARgamma S112 phosphorylation assay, PPARgamma-S112A genetic rescue, ERK inhibition, adipogenic differentiation assay Nature medicine High 18204460
2009 DOK1 PH domain binds phosphatidylinositol 5-phosphate (PtdIns5P) in vitro; DOK1 tyrosine phosphorylation correlates with PtdIns5P production in T cells upon TCR triggering. PtdIns5P increase regulates DOK1 tyrosine phosphorylation in vivo. The PH domain is necessary for DOK1 tyrosine phosphorylation and negative functions in T cells. In vitro lipid binding assay, intracellular PtdIns5P modulation, phosphorylation assay in T cells, PH domain deletion mutants Journal of immunology Medium 19299694
2009 CD45 recruits DOK1 to the proximal plasma membrane; DOK1-Y296F mutant abrogates interaction with CD45. CD45 expression is required for DOK1 membrane targeting in response to anti-CD3 stimulation. Stable expression of DOK1 decreases JAK-2 and STAT-3/5 phosphorylation following IL-3 and IFN-alpha stimulation; silencing DOK1 rescues MAP kinase and JAK activities in CD45-positive cells. Co-immunoprecipitation, site-directed mutagenesis (Y296F), stable overexpression, siRNA knockdown, JAK/STAT phosphorylation assay, membrane localization assay Molecular immunology Medium 19481264
2011 Oncogenic tyrosine kinases (p210(bcr-abl) and oncogenic Src) downregulate DOK1 by targeting it for ubiquitin-proteasome-mediated degradation; this process is tyrosine kinase activity-dependent and mediated primarily by lysine-dependent polyubiquitination. Restoration of DOK1 strongly suppresses transformation; a DOK1 mutant refractory to degradation shows stronger suppression. Proteasome inhibitor treatment, ubiquitination assay, DOK1 degradation-resistant mutant, transformation assay Molecular and cellular biology Medium 21536658
2014 BRK (breast tumor kinase/PTK6) interacts with and phosphorylates DOK1 specifically on Y362; this phosphorylation significantly downregulates DOK1 through the ubiquitin-proteasome pathway, promoting cell proliferation and migration. Co-immunoprecipitation, in vitro kinase assay (Y362 site-directed mutagenesis), ubiquitination assay, DOK1 protein stability assay, cell proliferation and migration assays PloS one Medium 24523872
2014 DOK1 regulates PDGF-BB-stimulated glioma cell invasion through tyrosine phosphorylation of p130Cas and activation of Rap1. DOK1 becomes tyrosine phosphorylated at Y362 and Y398 upon PDGF-BB stimulation; DOK1 knockdown or Y362F/Y398F double mutant inhibits both PDGF-BB-induced p130Cas phosphorylation and Rap1 activation. DOK1 co-localizes with phospho-p130Cas at the cell membrane. siRNA knockdown, DOK1 phosphosite mutant (DOK1FF), co-localization (immunofluorescence), Rap1 activation assay, 3D spheroid invasion assay Journal of cell science Medium 24762811
2016 DOK1 negatively regulates integrin alphaIIbbeta3 outside-in signaling in platelets (but not inside-out signaling). Dok-1-/- platelets show increased clot retraction, increased PLCgamma2 phosphorylation, and enhanced spreading on fibrinogen after thrombin stimulation. Dok-1-/- mice exhibit shortened bleeding times and accelerated carotid artery thrombosis. Dok-1-/- mouse, platelet functional assays (clot retraction, fibrinogen binding, P-selectin expression), PLCgamma2 phosphorylation assay, in vivo thrombosis model Thrombosis and haemostasis High 26790499
2023 The two SH2 domains of RasGAP (p120RasGAP) generate distinct binding interactions with doubly phosphorylated DOK1; RasGAP binding to DOK1 is ~100-fold stronger than to EphB4, driven by dual SH2 engagement with dominant N-SH2 interaction. RasGAP-DOK1 interactions do not impact RasGAP catalytic activity, implying RasGAP utilizes its SH2 domains to achieve spatial-temporal regulation of Ras signaling by localizing to DOK1. Affinity measurements, small-angle X-ray scattering, in vitro RasGAP activity assay The Journal of biological chemistry Medium 37507023
2000 SHIP1 forms a complex with DOK1 in BCR/ABL-transformed hematopoietic cells; this interaction requires the SH2 domain of SHIP1 and the PTB domain of DOK1. DOK1-SHIP1 association is mutually exclusive with DOK1-RasGAP association. The DOK1/SHIP1 complex is only detected in the cytosolic fraction. Co-immunoprecipitation, domain-deletion mutants, subcellular fractionation Cellular signalling Medium 10822173
2000 SH2D1A (XLP gene product) associates with DOK1 via its SH2 domain; this interaction depends on DOK1 phospho-Y449 in the sequence ALYSQVQK. An XLP-associated SH2D1A mutant fails to associate with DOK1. Overexpression of SH2D1A activates NF-kappaB (independent of SH2 domain, via IKKbeta). Co-immunoprecipitation, site-directed mutagenesis (XLP mutant SH2D1A), NF-kappaB reporter assay, dominant-negative IKKbeta Proceedings of the National Academy of Sciences of the United States of America Medium 10852966
1999 SHP-1 constitutively associates with p62(DOK) in bone marrow macrophages, and this association occurs independently of p62(DOK) tyrosine phosphorylation. The SHP-1 catalytic domain (identified via catalytically inert SHP-1 C453S trapping) directly binds tyrosine-phosphorylated p62(DOK). p62(DOK) is the major CSF-1R-associated tyrosine-phosphorylated protein in CSF-1-treated macrophages; hyperphosphorylation in SHP-1-deficient macrophages correlates with growth factor-independent survival. Co-immunoprecipitation, far Western analysis, SHP-1-deficient (motheaten) mice, CSF-1 stimulation assay The Journal of biological chemistry Medium 10585470
2015 Phosphorylated serine residues S745 and S756 (adjacent to the NxxF motif) in the integrin beta2 tail are required for DOK1 PTB domain interaction, providing an alternative phosphorylation switch for Dok1 binding to beta2 integrins (which lack a phosphorylatable NxxY motif). NMR analyses show higher affinity for the pSer756-containing beta2 peptide; the phosphorylated beta2 peptide occupies the canonical Dok1 PTB ligand-binding pocket. NMR spectroscopy, docking/structural modelling, cell-based binding assays Scientific reports Medium 26108885
2018 The scaffold protein 14-3-3zeta interacts with the PTB domain of DOK1 (mapped to beta-sheet region) independently of phosphorylated integrin beta CTs. The 14-3-3zeta/Dok1 binary complex can simultaneously bind cognate phosphorylated integrin beta CT sequences, with Thr-phosphorylated beta2 or beta3 CTs binding 14-3-3zeta and Ser-phosphorylated beta2 CT or Tyr-phosphorylated beta3 CT binding DOK1, suggesting a molecular switch for integrin regulation. NMR spectroscopy, co-immunoprecipitation, binding assays with phosphorylated peptides Journal of molecular biology Medium 30243836
2004 Frameshift mutation in DOK1 (GGCC deletion causing protein truncation) identified in CLL changes DOK1 from a cytoplasmic/membrane protein to a nuclear protein containing a functional bipartite nuclear localization signal. Mutant DOK1 fails to inhibit PDGF-induced MAP kinase activation and forms heterodimers with wild-type DOK1 (enhanced by Lck-mediated phosphorylation), indicating a dominant-negative mechanism. Heteroduplex analysis/sequencing, subcellular localization assay, MAP kinase assay, co-immunoprecipitation Oncogene Medium 14730347
2014 Dok1 and Dok2 are tyrosine phosphorylated upon NK cell activation; overexpression of Dok proteins in human NK cells reduces NK cell activation induced by activating receptors. Gene ablation of Dok1 and Dok2 in mice induces an NK cell maturation defect and leads to increased IFN-gamma production, establishing an intrinsic negative feedback loop downstream of NK cell activating receptors. Overexpression in human NK cells, Dok1/Dok2 double-knockout mice, NK cell maturation analysis, IFN-gamma production assay The EMBO journal Medium 24963146
2022 Upon FcεRI stimulation, DOK1 is recruited to the plasma membrane and undergoes tyrosine phosphorylation. Phosphorylated DOK1 inhibits FcεRI-operated calcium influx and negatively regulates mast cell degranulation by inhibiting calcium-dependent disassembly of actin filaments (F-actin disassembly). DOK1 overexpression in RBL-2H3 cells, co-immunoprecipitation, calcium influx assay, degranulation assay, F-actin staining Clinical immunology Medium 35421591

Source papers

Stage 0 corpus · 91 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 331 9008160
2000 The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells. Immunity 187 10755621
2001 Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation. The Journal of cell biology 142 11470823
2000 Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling. Genes & development 137 10640270
1999 Tyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migration. The EMBO journal 100 10202139
2007 An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding. The Journal of biological chemistry 97 18156175
2001 p62(dok), a negative regulator of Ras and mitogen-activated protein kinase (MAPK) activity, opposes leukemogenesis by p210(bcr-abl). The Journal of experimental medicine 96 11489947
2008 Dok1 mediates high-fat diet-induced adipocyte hypertrophy and obesity through modulation of PPAR-gamma phosphorylation. Nature medicine 92 18204460
2004 Role of Dok-1 and Dok-2 in myeloid homeostasis and suppression of leukemia. The Journal of experimental medicine 86 15611294
2007 Dok-1 and Dok-2 are negative regulators of T cell receptor signaling. International immunology 76 17329234
2005 Dok-1 and Dok-2 are negative regulators of lipopolysaccharide-induced signaling. The Journal of experimental medicine 74 15699069
2004 Role of Dok-1 and Dok-2 in leukemia suppression. The Journal of experimental medicine 74 15611295
2002 Downstream of kinase, p62(dok), is a mediator of Fc gamma IIB inhibition of Fc epsilon RI signaling. Journal of immunology (Baltimore, Md. : 1950) 69 11970986
2000 Domain-dependent function of the rasGAP-binding protein p62Dok in cell signaling. The Journal of biological chemistry 68 11042170
2004 c-Abl phosphorylates Dok1 to promote filopodia during cell spreading. The Journal of cell biology 62 15148308
2001 Phosphoinositide 3-kinase-dependent membrane recruitment of p62(dok) is essential for its negative effect on mitogen-activated protein (MAP) kinase activation. The Journal of experimental medicine 61 11489946
2002 Role of Dok1 in cell signaling mediated by RET tyrosine kinase. The Journal of biological chemistry 58 12087092
2000 Tyrosine phosphorylation of p62dok by p210bcr-abl inhibits RasGAP activity. Proceedings of the National Academy of Sciences of the United States of America 55 10688886
2009 Cutting edge: Dok-1 and Dok-2 adaptor molecules are regulated by phosphatidylinositol 5-phosphate production in T cells. Journal of immunology (Baltimore, Md. : 1950) 52 19299694
2004 Stromal cell-derived factor-1alpha/CXCL12-induced chemotaxis of T cells involves activation of the RasGAP-associated docking protein p62Dok-1. Blood 52 15345598
2001 Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt. The Journal of biological chemistry 48 11551902
2000 SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL. The Journal of biological chemistry 47 11031258
2009 Proteomic analysis of integrin alphaIIbbeta3 outside-in signaling reveals Src-kinase-independent phosphorylation of Dok-1 and Dok-3 leading to SHIP-1 interactions. Journal of thrombosis and haemostasis : JTH 46 19682241
2000 The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62dok (Dok1) and activates NF-kappa B. Proceedings of the National Academy of Sciences of the United States of America 46 10852966
2002 Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling. The Journal of biological chemistry 43 11825908
2002 The rasGAP-binding protein, Dok-1, mediates activin signaling via serine/threonine kinase receptors. The EMBO journal 43 11927552
2004 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 42 15574499
2004 DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells. The Journal of biological chemistry 41 15546884
1999 SHP-1 regulation of p62(DOK) tyrosine phosphorylation in macrophages. The Journal of biological chemistry 40 10585470
2006 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 39 16537894
2014 Dok1 and Dok2 proteins regulate natural killer cell development and function. The EMBO journal 35 24963146
2011 Characterization of DOK1, a candidate tumor suppressor gene, in epithelial ovarian cancer. Molecular oncology 32 21856257
2004 Dexamethasone up-regulates the inhibitory adaptor protein Dok-1 and suppresses downstream activation of the mitogen-activated protein kinase pathway in antigen-stimulated RBL-2H3 mast cells. Molecular pharmacology 32 15608142
2004 Functional interaction of RasGAP-binding proteins Dok-1 and Dok-2 with the Tec protein tyrosine kinase. Oncogene 31 14647425
2001 p62dok negatively regulates CD2 signaling in Jurkat cells. Journal of immunology (Baltimore, Md. : 1950) 31 11254695
2003 Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain. The Journal of biological chemistry 29 14607833
2000 Evidence that Llck-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling. The Journal of biological chemistry 29 10799545
2013 Differential role of Dok1 and Dok2 in TLR2-induced inflammatory signaling in glia. Molecular and cellular neurosciences 28 23659921
2011 Inactivation of the putative suppressor gene DOK1 by promoter hypermethylation in primary human cancers. International journal of cancer 28 21796618
2001 Inhibition of the motility and growth of B16F10 mouse melanoma cells by dominant negative mutants of Dok-1. Molecular and cellular biology 28 11463826
1998 Interactions of p62(dok) with p210(bcr-abl) and Bcr-Abl-associated proteins. The Journal of biological chemistry 26 9822717
2004 Frameshift mutation in the Dok1 gene in chronic lymphocytic leukemia. Oncogene 25 14730347
2002 Clustering the mast cell function-associated antigen (MAFA) leads to tyrosine phosphorylation of p62Dok and SHIP and affects RBL-2H3 cell cycle. Immunology letters 25 12008030
2000 Mediation by the protein-tyrosine kinase Tec of signaling between the B cell antigen receptor and Dok-1. The Journal of biological chemistry 25 10823839
2017 Anti-inflammation conferred by stimulation of CD200R1 via Dok1 pathway in rat microglia after germinal matrix hemorrhage. Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 24 28792282
2009 CD45 recruits adapter protein DOK-1 and negatively regulates JAK-STAT signaling in hematopoietic cells. Molecular immunology 24 19481264
2006 A nuclear export signal and phosphorylation regulate Dok1 subcellular localization and functions. Molecular and cellular biology 22 16705178
2004 Molecular basis of distinct interactions between Dok1 PTB domain and tyrosine-phosphorylated EGF receptor. Journal of molecular biology 22 15476828
2000 The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells. Cellular signalling 22 10822173
2015 Photoactivation of Dok1/ERK/PPARγ signaling axis inhibits excessive lipolysis in insulin-resistant adipocytes. Cellular signalling 21 25813581
2004 Dok-1 tyrosine residues at 336 and 340 are essential for the negative regulation of Ras-Erk signalling, but dispensable for rasGAP-binding. Genes to cells : devoted to molecular & cellular mechanisms 21 15189452
2016 RASSF1A and DOK1 Promoter Methylation Levels in Hepatocellular Carcinoma, Cirrhotic and Non-Cirrhotic Liver, and Correlation with Liver Cancer in Brazilian Patients. PloS one 20 27078152
2011 Oncogenic tyrosine kinases target Dok-1 for ubiquitin-mediated proteasomal degradation to promote cell transformation. Molecular and cellular biology 20 21536658
2014 Epstein-Barr virus down-regulates tumor suppressor DOK1 expression. PLoS pathogens 19 24809689
2014 A crucial role for DOK1 in PDGF-BB-stimulated glioma cell invasion through p130Cas and Rap1 signalling. Journal of cell science 18 24762811
2016 Dok1 and Dok2 Proteins Regulate Cell Cycle in Hematopoietic Stem and Progenitor Cells. Journal of immunology (Baltimore, Md. : 1950) 17 27183638
2014 BRK targets Dok1 for ubiquitin-mediated proteasomal degradation to promote cell proliferation and migration. PloS one 17 24523872
2005 Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation. Journal of immunology (Baltimore, Md. : 1950) 17 16177091
2012 Transcriptional regulation of the human tumor suppressor DOK1 by E2F1. Molecular and cellular biology 16 23028047
2006 Differential regulation of adapter proteins Dok2 and Dok1 in platelets, leading to an association of Dok2 with integrin alphaIIbbeta3. Journal of thrombosis and haemostasis : JTH 16 17092301
2001 T cell regulation of p62(dok) (Dok1) association with Crk-L. The Journal of biological chemistry 16 11553620
2017 Intratumoral Heterogeneity of Somatic Mutations for NRIP1, DOK1, ULK1, ULK2, DLGAP3, PARD3 and PRKCI in Colon Cancers. Pathology oncology research : POR 15 28844109
2017 DOK1/PPARgamma pathway mediates anti-tumor ability of all-trans retinoic acid in breast cancer MCF-7 cells. Biochemical and biophysical research communications 14 28396148
2015 An Alternative Phosphorylation Switch in Integrin β2 (CD18) Tail for Dok1 Binding. Scientific reports 14 26108885
2014 mRNA expression of DOK1-6 in human breast cancer. World journal of clinical oncology 13 24829863
2011 A computational analysis of the dynamic roles of talin, Dok1, and PIPKI for integrin activation. PloS one 13 22110576
2005 Dok1 expression and mutation in Burkitt's lymphoma cell lines. Cancer letters 12 16338067
2016 Dok-1 negatively regulates platelet integrin αIIbβ3 outside-in signalling and inhibits thrombosis in mice. Thrombosis and haemostasis 11 26790499
2005 Dok1 and SHIP act as negative regulators of v-Abl-induced pre-B cell transformation, proliferation and Ras/Erk activation. Cell cycle (Georgetown, Tex.) 11 15655368
2007 Dok-1 is a positive regulator of IL-4 signalling and IgE response. Journal of biochemistry 10 17827176
2004 High-level expression of Dok-1 in neurons of the primate prefrontal cortex and hippocampus. Journal of neuroscience research 10 14705142
2023 Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP, and Dok1. The Journal of biological chemistry 9 37507023
2018 Interaction Analyses of 14-3-3ζ, Dok1, and Phosphorylated Integrin β Cytoplasmic Tails Reveal a Bi-molecular Switch in Integrin Regulation. Journal of molecular biology 9 30243836
2017 Dok-1 and Dok-2 Are Required To Maintain Herpes Simplex Virus 1-Specific CD8+ T Cells in a Murine Model of Ocular Infection. Journal of virology 9 28490594
2012 The inositol 5-phosphatase SHIP-1 and adaptors Dok-1 and 2 play central roles in CD4-mediated inhibitory signaling. Immunology letters 9 22370159
2016 Dok-1 and Dok-2 Regulate the Formation of Memory CD8+ T Cells. Journal of immunology (Baltimore, Md. : 1950) 8 27664281
2014 NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters. PloS one 8 24587391
2011 Dok-1 and Dok-2 deficiency induces osteopenia via activation of osteoclasts. Journal of cellular physiology 8 21732353
2014 Phosphorylation of Dok1 by Abl family kinases inhibits CrkI transforming activity. Oncogene 7 25043303
2021 Expression of the EGFR-RAS Inhibitory Proteins DOK1 and MTMR7 and its Significance in Colorectal Adenoma and Adenoma Recurrence. Journal of gastrointestinal and liver diseases : JGLD 6 34941983
2020 Analysis of the DOK1 gene in breast cancer. Molecular biology reports 6 31919752
2012 Dok-1 overexpression promotes development of γδ natural killer T cells. European journal of immunology 6 22736313
2005 Germline mutations in Dok1 do not predispose to chronic lymphocytic leukemia. Leukemia research 6 15541476
2000 Priming of CD2-induced p62Dok tyrosine phosphorylation by CD3 in Jurkat T cells. European journal of immunology 6 11093148
2016 Loss of Dok-1 and Dok-2 in mice causes severe experimental colitis accompanied by reduced expression of IL-17A and IL-22. Biochemical and biophysical research communications 5 27450811
2024 DOK1 and DOK2 regulate CD8 T cell signaling and memory formation without affecting tumor cell killing. Scientific reports 4 38956389
2024 DOK1 facilitates the advancement of ccRCC. Journal of Cancer 4 39513119
2022 Dok-1 regulates mast cell degranulation negatively through inhibiting calcium-dependent F-actin disassembly. Clinical immunology (Orlando, Fla.) 4 35421591
2016 Expression of DOK1, 2, and 3 genes in HTLV-1-infected T cells. Acta virologica 3 27265473
2000 In vitro-generated stem cell leukaemia showing altered cell cycle progression with distinct signalling of the tyrosine-phosphorylated rasGAP-associated p62(dok) protein. The Journal of pathology 3 11054720
2004 Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein. Acta crystallographica. Section D, Biological crystallography 0 14747716

Missed literature

Know a paper Affinage missed for DOK1? Flag it for the maintainers and the community.

No submissions yet.