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Title: Tyrosine phosphorylation of SGEF regulates RhoG activity and cell migration
Authors: Okuyama, Yusuke
Umeda, Kentaro
Negishi, Manabu  kyouindb  KAKEN_id
Katoh, Hironori  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-8191-8117 (unconfirmed)
Author's alias: 加藤, 裕教
Issue Date: 1-Jul-2016
Publisher: Public Library of Science
Journal title: PLOS ONE
Volume: 11
Issue: 7
Thesis number: e0159617
Abstract: SGEF and Ephexin4 are members of the Ephexin subfamily of RhoGEFs that specifically activate the small GTPase RhoG. It is reported that Ephexin1 and Ephexin5, two well-characterized Ephexin subfamily RhoGEFs, are tyrosine-phosphorylated by Src, and that their phosphorylation affect their activities and functions. In this study, we show that SGEF, but not Ephexin4, is tyrosine-phosphorylated by Src. Tyrosine phosphorylation of SGEF suppresses its interaction with RhoG, the elevation of RhoG activity, and SGEF-mediated promotion of cell migration. We identified tyrosine 530 (Y530), which is located within the Dbl homology domain, as a major phosphorylation site of SGEF by Src, and Y530F mutation blocked the inhibitory effect of Src on SGEF. Taken together, these results suggest that the activity of SGEF is negatively regulated by tyrosine phosphorylation of the DH domain.
Rights: © 2016 Okuyama et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
URI: http://hdl.handle.net/2433/216371
DOI(Published Version): 10.1371/journal.pone.0159617
PubMed ID: 27437949
Appears in Collections:Journal Articles

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