Scientific Report
- EMBO reports (2009) 10, 851 - 856
- doi:10.1038/embor.2009.96
Published online: 26 June 2009
Subject Category:
Coiled-coil interactions are required for post-Golgi R-SNARE trafficking
David E Gordon1,*, Myriam Mirza1,*†, Daniela A Sahlender1, Jovana Jakovleska1,‡ & Andrew A Peden1
- Department of Clinical Biochemistry, University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB20XY, UK
Correspondence to:
Andrew A Peden, Tel: +44 (0)1223 763 218; Fax: +44 (0)1223 762 640; E-mail: aap2@cam.ac.uk
†Present address: Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G1Y6
‡Present address: Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany
*These authors contributed equally to this work
Received 30 September 2008; Revised 3 April 2009; Accepted 7 April 2009
Abstract
The sorting of post-Golgi R-SNAREs (vesicle-associated membrane protein (VAMP)1, 2, 3, 4, 7 and 8) is still poorly understood. To address this, we developed a system to investigate their localization, trafficking and cell-surface levels. Here, we show that the distribution and internalization of VAMPs 3 and 8 are determined solely through a new conserved mechanism that uses coiled-coil interactions, and that VAMP4 does not require these interactions for its trafficking. We propose that VAMPs 3 and 8 are trafficked while in a complex with Q-SNAREs. We also show that the dileucine motif of VAMP4 is required for both its internalization and retrieval to the trans-Golgi network. However, when the dileucine motif is mutated, the construct can still be internalized potentially through coiled-coil interactions with Q-SNAREs.
Keywords:
- SNARE,
- VAMP3,
- VAMP4,
- VAMP7,
- VAMP8
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