DOCK1 Antibody

1. High DOCK1 expression is associated with Oral squamous cell carcinoma. PMID: 29286141
2. Dock1 modulation by miR-31 plays an important function in glioma invasion PMID: 26946516
3. In summary, this investigation identifies an EGFR-DOCK180-RAC1-MLK3-JNK signaling axis that drives glioblastoma cell migration and dissemination.IMPLICATIONS: On the basis of these findings, MLK3 emerges as a potential therapeutic target for the treatment of glioblastoma PMID: 28487380
4. one statistically significant common variant in the DOCK1 gene was associated with DeltaBMI in GI cancer and COPD cases providing support for at least partially shared aetiology of DeltaBMI in complex diseases. PMID: 28044437
5. Taken together, these results indicate that DOCK1 is a critical regulator of the malignant phenotypes induced by Rac1(P29S), and suggest that targeting DOCK1 might be an effective approach to treat cancers associated with Rac1(P29S) mutation. PMID: 29432733
6. Data suggest that GPR124 promotes cell adhesion via interaction with Elmo1-Dock180 and intersectin 1/2; this constitutes a previously unrecognized heteromeric complex that is putatively involved in GPR124-dependent adhesive/angiogenic responses in vascular endothelial cells. (GPR124 = G-protein coupled receptor 124; Elmo1 = ELMO domain-containing protein 1; Dock180 = dedicator of cytokinesis protein 1 180 kDa) PMID: 28600358
7. stimulation of the DOCK180 pathway represents an alternative mechanism of PTP1B inhibitor-stimulated endothelial cell motility, which does not require concomitant VEGFR2 activation as a prerequisite. PMID: 27052191
8. Thus, Elmo1 and Dock180 facilitate blood vessel formation by stabilization of the endothelium during angiogenesis. PMID: 25586182
9. High DOCK180 expression is associated with serous ovarian cancer. PMID: 24819662
10. our findings describe a novel mechanism by which EGFRvIII drives glioma tumorigenesis and invasion through protein kinase A-dependent phosphorylation of Dock180 PMID: 23728337
11. findings indicate that a chemokine-controlled pathway, consisting of Galphai2, ELMO1/Dock180, Rac1 and Rac2, regulates the actin cytoskeleton during breast cancer metastasis PMID: 23591873
12. Dock180 could act as a pro-survival molecule in H9C2 cardiomyocytes via activation of its downstream pro-survival signaling molecule, AKT. PMID: 23314417
13. Solved is the solution structure of DOCK180 SH3 domain, which shares similar target binding features with the SH3 domain of DOCK2. PMID: 23239367
14. DOCK1-Rac signaling as an HER2 effector pathway essential for HER2-mediated breast cancer progression to metastasis. PMID: 23592719
15. Phosphorylation of Dock180(Y1811) enhanced its association with CrkII & p130(Cas). Dock180 associated with PDGFRalpha to promote cell migration. Phosphorylated Dock180(Y1811) contributes to activation of Rac1 in human cancers with PDGFRA amplification. PMID: 22080864
16. EGFRvIII (also known as DeltaEGFR and de2-7EGFR), a constitutively active EGFR mutant that is frequently co-overexpressed with EGFR in human glioblastoma, promotes tumorigenesis through Src family kinase (SFK)-dependent phosphorylation of Dock180 PMID: 22323579
17. Dock180 contributes to ovarian carcinogenesis and dissemination PMID: 22175896
18. DOCK180, an atypical Rac activator, links CXCR4 signaling to Rac activation in order to control endothelial cell migration during cardiovascular development. PMID: 20829512
19. protein-protein interaction mediated by ARNO coiled-coil domain required for ARNO induced motility; coiled-coil domain promotes assembly of multiprotein complex containing ARNO and Dock180; assembly of complex requires coiled-coil domain, GRASP and IPCEF PMID: 20016009
20. Dock180 ELMO complex functions as an unconventional two-part exchange factor for Rac. PMID: 12134158
21. identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity PMID: 12432077
22. Rac activation by the ELMO.Dock180 complex at discrete intracellular locations mediated by the N-terminal 330 amino acids of ELMO1 plays a role in cell migration PMID: 14638695
23. The N-terminal SH3 domain of Dock180 binds to the distant catalytic Docker domain and negatively regulates the function of Dock180. PMID: 15723800
24. DOCK180, via its DHR-1 and DHR-2 domains, couples PtdIns(3,4,5)P(3) signalling to Rac GTP-loading, which is essential for directional cell movement. PMID: 16025104
25. ARNO and ARF6 coordinate with the Dock180/Elmo complex to promote Rac activation at the leading edge of migrating cells. PMID: 16213822
26. The DOCK180 protein is ubiquitylated on the plasma membrane, and also that Elmo1 functions as an inhibitor of ubiquitylation of Dock180. PMID: 16495483
27. Using pulldown assays, we identified engulfment and cell motility (ELMO) protein as the IpgB1 binding partner. IpgB1 colocalized with ELMO and Dock180 in membrane ruffles induced by Shigella. PMID: 17173036
28. A significant percentage of the total endogenous Crk II partitions in the nucleus in mammalian cells, where it forms distinct complexes with DOCK180, Wee1, and Abl. PMID: 17764157
29. DOCK180 regulates CI-MPR trafficking via SNX5 and this function is independent of its guanine nucleotide exchange factor activity toward Rac1 PMID: 18596235
30. The DOCK180-ELMO1 interaction is mapped to the N-terminal 200 amino acids of DOCK180, and to the C-terminal 200 amino acids of ELMO1, comprising the ELMO1 PH domain. PMID: 18768751
31. ANKRD28, a novel binding partner of DOCK180, promotes cell migration by regulating focal adhesion formation. PMID: 19118547
32. It regulates cell morphology and motility. (review) PMID: 19803396

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HGNC: 2987

OMIM: 601403

KEGG: hsa:1793

STRING: 9606.ENSP00000280333

UniGene: Hs.159195