PKD is recruited to sites of actin remodelling at the leading edge and negatively regulates cell migration

FEBS Lett. 2007 Sep 4;581(22):4279-87. doi: 10.1016/j.febslet.2007.07.079. Epub 2007 Aug 10.


Protein kinase D (PKD) has been implicated in the regulation of cell shape, adhesion, and migration. At the leading edge of migrating cells active PKD co-localizes with F-actin, Arp3 and cortactin. Platelet derived growth factor (PDGF) activates PKD and recruits the kinase to the leading edge, suggesting a role for PKD in actin remodelling. In support of this, PKD directly interacts with F-actin and phosphorylates cortactin in vitro. Interference with PKD function by overexpression of a dominant negative PKD or by PKD-specific siRNA enhanced cell migration, whereas cells overexpressing PKD wild type displayed reduced migratory potential. Taken together, these data reveal a negative regulatory function of PKD in cell migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Cell Movement*
  • Cortactin / metabolism
  • Mice
  • Phosphorylation
  • Protein Binding
  • Protein Kinase C / metabolism*
  • Protein Transport
  • Pseudopodia / enzymology*


  • Actins
  • Cortactin
  • protein kinase D
  • Protein Kinase C