Article
- The EMBO Journal (2008) 27, 1423 - 1435
- doi:10.1038/emboj.2008.75
Published online: 17 April 2008
Subject Category:
Yeast and human Ysl2p/hMon2 interact with Gga adaptors and mediate their subcellular distribution
Birgit Singer-Krüger1,
Maja Lasi
1,
Anna-Maria Bürger1,
Angelika Hau
er2,
Rüdiger Pipkorn3 and Yi Wang1
- Institute for Biochemistry, University of Stuttgart, Stuttgart, Germany
- Institute of Cell Biology and Immunology, University of Stuttgart, Stuttgart, Germany
- Deutsches Krebsforschungszentrum, Heidelberg, Germany
Correspondence to:
Birgit Singer-Krüger, Institute for Biochemistry, University of Stuttgart, Pfaffenwaldring 55, Stuttgart 70569, Germany. Tel.: +49 711 685 64387; Fax: +49 711 685 64392; E-mail: Singer-Krueger@ibc.uni-stuttgart.de
Received 24 September 2007; Accepted 19 March 2008
Abstract
The Gga proteins represent a family of ubiquitously expressed clathrin adaptors engaged in vesicle budding at the tubular endosomal network/trans Golgi network. Their membrane recruitment is commonly thought to involve interactions with Arf and signals in cargo through the so-called VHS domain. For yeast Gga proteins, however, partners binding to its VHS domain have remained elusive and Gga localization does not absolutely depend on Arf. Here, we demonstrate that yeast Gga recruitment relies on a network of interactions between the scaffold Ysl2p/Mon2p, the small GTPase Arl1p, and the flippase Neo1p. Deletion of either YSL2 or ARL1 causes mislocalization of Gga2p, whereas a neo1-69 mutant accumulates Gga2p on aberrant structures. Remarkably, Ysl2p directly interacts with human and yeast Ggas through the VHS domain, and binding to Gga proteins is also found for the human Ysl2p orthologue hMon2. Thus, Ysl2p represents an essential, evolutionarily conserved member of a network controlling direct binding and membrane docking of Ggas. Because activated Arl1p is part of the network that binds Gga2p, Arf and Arf-like GTPases may interact in a regulatory cascade.
Keywords:
- Arf family,
- clathrin coat,
- endosomes,
- flippase,
- membrane traffic
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