Integrin regulation of cell signalling and motility.

  title={Integrin regulation of cell signalling and motility.},
  author={Rudolph L Juliano and Peter J. Reddig and Suresh K. Alahari and Matthew L. Edin and Alan K. Howe and Andrew E. Aplin},
  journal={Biochemical Society transactions},
  volume={32 Pt3},
Integrins clearly play a key role in regulating both mitogenic signalling and cell migration. Thus integrins modulate the efficiency of the Erk (extracellular-signal-regulated kinase)/MAP kinase (mitogen-activated protein kinase) pathway, acting at several distinct levels. We have shown that both cAMP-dependent protein kinase and PAKs (p21-activated kinases) play a role in integrin regulation of the Erk pathway, acting primarily at the level of Raf-1. Integrins and PAKs also play a role in the… 

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Arch. Biochem. Biophys. J. Biol. Chem

  • Arch. Biochem. Biophys. J. Biol. Chem
  • 2002

Nature Exp. Cell Res

  • Nature Exp. Cell Res
  • 1997

J. Cell Sci. Exp. Cell Res

  • J. Cell Sci. Exp. Cell Res
  • 1999

J. Cell Biol. Biochem. J. Mol. Cell. Biol

  • J. Cell Biol. Biochem. J. Mol. Cell. Biol
  • 1997

Nat. Cell Biol. J. Cell Sci. EMBO J. Mol. Cell. Biol

  • Nat. Cell Biol. J. Cell Sci. EMBO J. Mol. Cell. Biol
  • 2001

J. Cell Sci

  • J. Cell Sci
  • 2002


  • EMBO J
  • 2000