Pkd is Recruited to Sites of Actin Remodelling at the Leading Edge and Negatively Regulates Cell Migration.
From: Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
FEBS letters
- Publish Date: Sep 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 22
- Pages: 4279-87
- Medium: Print
- Language: English
- Citation (JAMA): Eiseler Tim, Schmid Michael A, Topbas Fitnat, et al. Pkd is Recruited to Sites of Actin Remodelling at the Leading Edge and Negatively Regulates Cell Migration.. FEBS Lett. Sep 2007;581:4279-87
Abstract
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.
Mesh Headings (Keywords): Actins, Animals, Cell Movement, Cortactin, Mice, Phosphorylation, Protein Binding, Protein Kinase C, Protein Transport, Pseudopodia
Check for Full Text / PubMed Unique Identifier (PMID): 17707375
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.