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DOCK1 — SRC
Pathways - manually collected, often from reviews:
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
None
→
FAK/Src-Yes-Fyn/p130 CAS/CRK/DOCK1/ELMO1 complex (PTK2-YES1_SRC_FYN-BCAR1-CRK-DOCK1-ELMO1)
(modification, collaborate)
Cho et al., J Cell Biol 2002, Hsia et al., J Cell Biol 2003, Sharma et al., BMC cell biology 2008, Kiyokawa et al., Genes Dev 1998, Dolfi et al., Proc Natl Acad Sci U S A 1998
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
RAC1/GDP complex (RAC1)
→
FAK/Src-Yes-Fyn/p130 CAS/CRK/DOCK1/ELMO1 complex (PTK2-YES1_SRC_FYN-BCAR1-CRK-DOCK1-ELMO1)
(modification, collaborate)
Cho et al., J Cell Biol 2002, Hsia et al., J Cell Biol 2003, Sharma et al., BMC cell biology 2008, Kiyokawa et al., Genes Dev 1998, Dolfi et al., Proc Natl Acad Sci U S A 1998
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
FAK/Src-Yes-Fyn/p130 CAS/CRK/DOCK1/ELMO1 complex (PTK2-YES1_SRC_FYN-BCAR1-CRK-DOCK1-ELMO1)
→
None
(modification, activates)
Cho et al., J Cell Biol 2002, Hsia et al., J Cell Biol 2003, Sharma et al., BMC cell biology 2008, Kiyokawa et al., Genes Dev 1998, Dolfi et al., Proc Natl Acad Sci U S A 1998
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
FAK/Src-Yes-Fyn/p130 CAS/CRK/DOCK1/ELMO1 complex (PTK2-YES1_SRC_FYN-BCAR1-CRK-DOCK1-ELMO1)
→
DOCK1/ELMO1 complex (DOCK1-ELMO1)
(modification, collaborate)
Hsia et al., J Cell Biol 2003
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
FAK/Src-Yes-Fyn/p130 CAS/CRK/DOCK1/ELMO1 complex (PTK2-YES1_SRC_FYN-BCAR1-CRK-DOCK1-ELMO1)
→
FAK/Src-Yes-Fyn/p130 CAS/CRK complex (PTK2-YES1_SRC_FYN-BCAR1-CRK)
(modification, collaborate)
Hsia et al., J Cell Biol 2003
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Signaling events mediated by focal adhesion kinase:
DOCK1/ELMO1 complex (DOCK1-ELMO1)
→
FAK/Src-Yes-Fyn/p130 CAS/CRK complex (PTK2-YES1_SRC_FYN-BCAR1-CRK)
(modification, collaborate)
Hsia et al., J Cell Biol 2003
Evidence: mutant phenotype, physical interaction
-
Reactome Reaction:
SRC
→
DOCK1
(indirect_complex)
Shekarabi et al., Mol Cell Neurosci 2002, Li et al., J Biol Chem 2002, Vallés et al., J Biol Chem 2004, Shekarabi et al., J Neurosci 2005, Li et al., Nat Neurosci 2008, Briançon-Marjollet et al., Mol Cell Biol 2008
-
Reactome Reaction:
SRC
→
DOCK1
(reaction)
Shekarabi et al., Mol Cell Neurosci 2002, Li et al., J Biol Chem 2002, Vallés et al., J Biol Chem 2004, Shekarabi et al., J Neurosci 2005, Li et al., Nat Neurosci 2008, Briançon-Marjollet et al., Mol Cell Biol 2008
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Feng et al., J Clin Invest 2011
(Brain Neoplasms...) :
Activation of Rac1 by
Src dependent phosphorylation of
Dock180 ( Y1811 ) mediates PDGFRa stimulated glioma tumorigenesis in mice and humans ... Here, we report that PDGFRa signaling in glioblastomas leads to
Src dependent phosphorylation of the guanine nucleotide exchange factor
Dock180 at tyrosine 1811 ( Dock180 ( Y1811 ) ) that results in activation of the GTPase Rac1 and subsequent cell growth and invasion
Feng et al., Proc Natl Acad Sci U S A 2012
(Cell Transformation, Neoplastic...) :
Here, we report that EGFRvIII ( also known as dEGFR 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 , a guanine nucleotide exchange factor for Rac1 ... The SFKs,
Src , Fyn, and Lyn, induce phosphorylation of Dock180 ( Y722 ) and inhibition of these SFKs by pharmacological inhibitors or shRNA depletion markedly
attenuates EGFRvIII induced phosphorylation of
Dock180 ( Y722 ), Rac1 activity, and glioblastoma cell migration