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Human Polyclonal DOCK1 Primary Antibody for WB - ABIN257645
Hasegawa, Kiyokawa, Tanaka, Nagashima, Gotoh, Shibuya, Kurata, Matsuda: DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane. in Molecular and cellular biology 1996
High DOCK1 expression is associated with Oral squamous cell carcinoma.
Dock1 modulation by miR-31 plays an important function in glioma invasion
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
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.
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.
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)
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.
Thus, Elmo1 and Dock180 facilitate blood vessel formation by stabilization of the endothelium during angiogenesis.
High DOCK180 expression is associated with serous ovarian cancer.
our findings describe a novel mechanism by which EGFRvIII drives glioma tumorigenesis and invasion through protein kinase A-dependent phosphorylation of Dock180
findings indicate that a chemokine-controlled pathway, consisting of Galphai2, ELMO1/Dock180, Rac1 and Rac2, regulates the actin cytoskeleton during breast cancer metastasis
Dock180 could act as a pro-survival molecule in H9C2 cardiomyocytes via activation of its downstream pro-survival signaling molecule, AKT.
Solved is the solution structure of DOCK180 SH3 domain, which shares similar target binding features with the SH3 domain of DOCK2.
DOCK1-Rac signaling as an HER2 effector pathway essential for HER2-mediated breast cancer progression to metastasis.
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.
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
Dock180 contributes to ovarian carcinogenesis and dissemination
DOCK180, an atypical Rac activator, links CXCR4 signaling to Rac activation in order to control endothelial cell migration during cardiovascular development.
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
signal transfer of Crk/Dock180/Rac1 is implicated in actin cytoskeleton reorganization and thus in the cell proliferation, motility, invasion, and of human ovarian cancer cell line SKOV3.
Inactivation of Dock1 in mammary gland epithelial cells and activation of Stat3 coincide with a delay in the initiation of mammary gland involution.
Dock1 and Dock5 are not the important exchange factors regulating Rac activity during the establishment and maintenance of the glomerular barrier
The phospholipase D-PA axis selectively controls dorsal ruffle formation by regulating DOCK1 localization.
The data demonstrate the ability of the SH3 domain of DOCK180 to interact with ELMO1, regardless of the presence of the polyproline-containing C-terminal end.
Dock1 has an essential role in embryonic development.
Results indicate that the combination of DOCK2 and DOCK180 plays a significant but not essential role in prevascular fetal thymus colonization.
This study demonstrated that Mutations in dock1 disrupt early Schwann cell development.
A novel signaling cascade is identified in which ELMO1/DOCK180 regulates vasculature formation in zebrafish.
The fusion of embryonic fast-twitch myoblasts requires the activities of Dock1 and the closely related Dock5 protein.
This gene product binds to the SH3 domain of CRK protein. It may regulate cell surface extension and may have a role in the cell surface extension of an engulfing cell around a dying cell during apoptosis.
180 kDa protein downstream of CRK
, DOwnstream of CrK
, dedicator of cyto-kinesis 1
, dedicator of cytokinesis protein 1
, dedicator of cytokinesis 1
, dedicator of cytokinesis protein 1-like