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JXB Advance Access published online on June 10, 2009
Journal of Experimental Botany, doi:10.1093/jxb/erp155
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

A novel di-acidic motif facilitates ER export of the syntaxin SYP31

Laurent Chatre1,2 * {dagger}, Valérie Wattelet-Boyer1 {dagger}, Su Melser1, Lilly Maneta-Peyret1, Federica Brandizzi2,3 {ddagger} and Patrick Moreau1,4 {ddagger},$

1University of Bordeaux 2, Membrane Biogenesis Laboratory, CNRS UMR 5200, 146, rue Léo Saignat, 33076 Bordeaux Cedex, France
2Department of Biology, University of Saskatchewan, Saskatoon, Canada
3Michigan State University-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA
4Imaging platform of the IFR 103, INRA-Bordeaux, France

$ To whom correspondence should be addressed: E-mail: Patrick.Moreau{at}biomemb.u-bordeaux2.fr

It is generally accepted that ER protein export is largely influenced by the transmembrane domain (TMD). The situation is unclear for membrane-anchored proteins such as SNAREs, which are anchored to the membrane by their TMD at the C-terminus. For example, in plants, Sec22 and SYP31 (a yeast Sed5 homologue) have a 17 aa TMD but different locations (ER/Golgi and Golgi), indicating that TMD length alone is not sufficient to explain their targeting. To establish the identity of factors that influence SNARE targeting, mutagenesis and live cell imaging experiments were performed on SYP31. It was found that deletion of the entire N-terminus domain of SYP31 blocked the protein in the ER. Several deletion mutants of different parts of this N-terminus domain indicated that a region between the SNARE helices Hb and Hc is required for Golgi targeting. In this region, replacement of the aa sequence MELAD by GAGAG or MALAG retained the protein in the ER, suggesting that MELAD may function as a di-acidic ER export motif EXXD. This suggestion was further verified by replacing the established di-acidic ER export motif DLE of a type II Golgi protein AtCASP and a membrane-anchored type I chimaera, TMcCCASP, by MELAD or GAGAG. The MELAD motif allowed the proteins to reach the Golgi, whereas the motif GAGAG was found to be insufficient to facilitate ER protein export. Our analyses indicate that we have identified a novel and transplantable di-acidic motif that facilitates ER export of SYP31 and may function for type I and type II proteins in plants.

Key words: Di-acidic motif, ER export, ER–Golgi interface, SNARE, syntaxin

* Present address: Institut Pasteur, Unité de Génétique Moléculaire des levures, 25–28 rue du Dr Roux, 75724 Paris cedex 15, France.

{dagger} Co-first authors.

{ddagger} Both laboratories contributed equally.

Received 30 October 2008; Revised 16 March 2009 Accepted 16 April 2009


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