ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner.

@article{StaceyTT2004ARAP3IT,
  title={ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner.},
  author={I StaceyT.T. and Zhongzhen Nie and Ashley H Stewart and Meri Najdovska and Nathan E. Hall and Hong He and Paul A Randazzo and Peter Lock},
  journal={Journal of cell science},
  year={2004},
  volume={117 Pt 25},
  pages={
          6071-84
        }
}
ARAP3 is a GTPase activating protein (GAP) for Rho and Arf GTPases that is implicated in phosphoinositide 3-kinase (PI 3-kinase) signalling pathways controlling lamellipodia formation and actin stress fibre assembly. We have identified ARAP3 as a phosphorylated target of protein tyrosine kinases. In cells, ARAP3 was tyrosine phosphorylated when co-expressed with Src-family kinases (SFKs), upon stimulation with growth factors and during adhesion to the extracellular matrix (ECM) substrate… CONTINUE READING

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