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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
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1437-4315
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Volume 389, Issue 4

Issues

Smurf1 directly targets hPEM-2, a GEF for Cdc42, via a novel combination of protein interaction modules in the ubiquitin-proteasome pathway

Kei Yamaguchi
  • 1Graduate School of Science and Technology, Chiba University, 648 Matsudo, Matsudo, Chiba 271-8510, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Osamu Ohara
  • 2Department of Human Genome Research, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu, Chiba 292-0818, Japan and Laboratory of Immunogenomics, RIKEN Yokohama Institute, 1-7-22 Suehiro, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Akikazu Ando
  • 3Graduate School of Science and Technology, Chiba University, 648 Matsudo, Matsudo, Chiba 271-8510, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Takahiro Nagase
  • 4Department of Human Genome Research, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu, Chiba 292-0818, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-03-27 | DOI: https://doi.org/10.1515/BC.2008.036

Abstract

Smurf1, a member of HECT-type E3 ubiquitin ligases, regulates cell polarity and protrusive activity by inducing ubiquitination and subsequent proteasomal degradation of the small GTPase RhoA. We report here that hPEM-2, a guanine nucleotide exchange factor for the small GTPase Cdc42, is a novel target of Smurf1. Pulse-chase labeling and a ubiquitination experiment using MG132, a proteasomal inhibitor, indicate that Smurf1 induces proteasomal degradation of hPEM-2 in cells. GST pull-down assays with heterologously expressed firefly luciferase-fusion proteins that include partial sequences of hPEM-2 reveal that part of the PH domain (residues 318–343) of hPEM-2 is sufficient for binding to Smurf1. In contrast, the hPEM-2 binding domain in Smurf1 was mapped to the C2 domain. Although it has been reported that the binding activities of some C2 domains to target proteins are regulated by Ca2+, Smurf1 interacts with hPEM-2 in a Ca2+-independent manner. Our discovery that hPEM-2 is, in addition to RhoA, a target protein of Smurf1 suggests that Smurf1 plays a crucial role in the spatio-temporal regulation of Rho GTPase family members.

Keywords: C2 domain; E3 ubiquitin ligase; guanine nucleotide exchange factor; HECT domain; PH domain; Rho signaling pathway

About the article

Corresponding author


Received: 2007-08-22

Accepted: 2007-12-18

Published Online: 2008-03-27

Published in Print: 2008-04-01


Citation Information: Biological Chemistry, Volume 389, Issue 4, Pages 405–413, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2008.036.

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