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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 392, Issue 3

Issues

Identification and characterisation of novel Mss4-binding Rab GTPases

Viktor Wixler
  • Institute of Molecular Virology, Münster University Hospital, Von Esmarch-Str. 56, D-48149 Münster, Germany
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Ludmilla Wixler
  • Institute of Molecular Virology, Münster University Hospital, Von Esmarch-Str. 56, D-48149 Münster, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Anika Altenfeld / Stephan Ludwig
  • Institute of Molecular Virology, Münster University Hospital, Von Esmarch-Str. 56, D-48149 Münster, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Roger S. Goody / Aymelt Itzen
  • Max-Planck-Institute of Molecular Physiology, Otto-Hahn Str. 11, D-44227 Dortmund, Germany
  • These authors contributed equally to this work.
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2011-06-18 | DOI: https://doi.org/10.1515/bc.2011.022

Abstract

The Mss4 (mammalian suppressor of yeast Sec4) is an evolutionarily highly conserved protein and is expressed in all mammalian tissues. Although its precise biological function is still elusive, it has been shown to associate with a subset of secretory Rab proteins (Rab1b, Rab3a, Rab8a, Rab10) and to possess a rather low guanine nucleotide exchange factor (GEF) activity towards them in vitro (Rab1, Rab3a and Rab8a). By screening a human placenta cDNA library with Mss4 as bait, we identified several Rab GTPases (Rab12, Rab13 and Rab18) as novel Mss4-binding Rab proteins. Only exocytic but no endocytic Rab GTPases were found in our search. The binding of Mss4 to Rab proteins was confirmed by direct yeast two-hybrid interaction, by co-immunoprecipitation from lysates of mammalian cells, by immunofluorescence colocalisation as well as by direct in vitro binding studies. Analysis of Mss4 catalytic activity towards different Rab substrates confirmed that it is a somewhat inefficient GEF. These data, together with our mutational analysis of Mss4-Rab binding capacity, support the already proposed idea that Mss4 functions rather as a chaperone for exocytic Rab GTPases than as a GEF.

Keywords: Dss4; GEF; Mss4; Rab

About the article

Corresponding author


Received: 2010-08-06

Accepted: 2010-10-19

Published Online: 2011-06-18

Published in Print: 2011-03-01


Citation Information: Biological Chemistry, Volume 392, Issue 3, Pages 239–248, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2011.022.

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