Crk–p130Cas complexes regulate cell spreading after integrin stimulation and serve as amolecular switch for induction of cell migration
DOCK1 is suggested to be the downstream effector of Crk in integrin signaling:
-DOCK1 binds to Crk after integrin stimulation;
-DOCK1 colocalizes with the Crk2–p130Cas complexes at focal adhesions and at the sites of membrane spreading;
-Expression of DOCK1 accelerates the formation of the Crk–p130Cas complexes.
It is likely that the DOCK1 recruited to the Crk–p130Cas complexes on integrin stimulation transduces signals to Rac1 at focal adhesions, which eventually induces cell spreading.
e_re981( EMT ):
Src and FAK kinases cooperate to phosphorylate paxillin, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.
Phosphorylated paxillin binding to Crk is implicated in Rac activation and stimulation of cell motility
CRK bound to DOCK1 (so-called DOCK180) forms complex with phosphorylated paxillin.
The complex is necessary for collagen-dependent cell migration, mainly through Rac1 activation.
Participates in complexes:
In compartment: Cytoplasm
Participates in reactions:
As Reactant or Product:
- PXN|pho@Cytoplasm + CRK@Cytoplasm + DOCK1@Cytoplasm → CRK:DOCK1:PXN|pho@Cytoplasm
- CRK:DOCK1:PXN|pho@Cytoplasm → Membrane spreading@Cytoplasm