| Literature DB >> 21087603 |
Rolf-Peter Scholz1, Johan O R Gustafsson, Peter Hoffmann, Mamta Jaiswal, Mohammed Reza Ahmadian, Stephan A Eisler, Patrik Erlmann, Simone Schmid, Angelika Hausser, Monilola A Olayioye.
Abstract
Deleted in liver cancer 1 (DLC1) is a tumor suppressor protein that is frequently downregulated in various tumor types. DLC1 contains a Rho GTPase activating protein (GAP) domain that appears to be required for its tumor suppressive functions. Little is known about the molecular mechanisms that regulate DLC1. By mass spectrometry we have mapped a novel phosphorylation site within the DLC1 GAP domain on serine 807. Using a phospho-S807-specific antibody, our results identify protein kinase D (PKD) to phosphorylate this site in DLC1 in intact cells. Although phosphorylation on serine 807 did not directly impact on in vitro GAP activity, a DLC1 serine-to-alanine exchange mutant inhibited colony formation more potently than the wild type protein. Our results thus show that PKD-mediated phosphorylation of DLC1 on serine 807 negatively regulates DLC1 cellular function. Copyright ÂEntities:
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Year: 2010 PMID： 21087603 DOI： 10.1016/j.yexcr.2010.11.003
Source DB: PubMed Journal: Exp Cell Res ISSN： 0014-4827 Impact factor: 3.905