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

, , , , und . FEBS Letters 581 (22): 4279--4287 (2007)

Zusammenfassung

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. © 2007 Federation of European Biochemical Societies.

Links und Ressourcen

DOI:
10.1016/j.febslet.2007.07.079
URL:
BibTeX-Schlüssel:
Eiseler2007
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