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https://hdl.handle.net/2440/66709
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Type: | Journal article |
Title: | The tumor suppressor protein DLC1 is regulated by PKD-mediated GAP domain phosphorylation |
Author: | Scholz, R. Gustafsson, O. Hoffmann, P. Jaiswal, M. Ahmadian, M. Eisler, S. Erlmann, P. Schmid, S. Hauser, A. Olayioye, M. |
Citation: | Experimental Cell Research, 2011; 317(4):496-503 |
Publisher: | Academic Press Inc Elsevier Science |
Issue Date: | 2011 |
ISSN: | 0014-4827 1090-2422 |
Statement of Responsibility: | Rolf-Peter Scholz, 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. |
Keywords: | Deleted in liver cancer 1 (DLC1) Protein kinase D (PKD) GTPase activating protein Rho signaling Serine phosphorylation Tumor suppressor |
Rights: | Copyright © 2010 Elsevier Inc. All rights reserved. |
DOI: | 10.1016/j.yexcr.2010.11.003 |
Published version: | http://dx.doi.org/10.1016/j.yexcr.2010.11.003 |
Appears in Collections: | Aurora harvest 5 Molecular and Biomedical Science publications |
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