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MBC in Press, published online ahead of print May 3, 2003
Mol. Biol. Cell 10.1091/mbc.E02-11-0736

A more recent version of this article appeared on August 1, 2003
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Submitted on November 16, 2002
Revised on March 23, 2003
Accepted on March 23, 2003

Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in S. cerevisiae

Thomas Sandmann1, Johannes M. Herrmann2, Jörn Dengjel3, Heinz Schwarz4, and Anne Spang1*

1 Friedrich Miescher Laboratorium der Max Planck Gesellschaft, Spemannstrasse 39, D-72076 Tübingen, Germany
2 Institut für Physiologische Chemie, Universität München, 81377 München, Germany
3 Institut für Immunologie, Universität Tübingen, D-72076 Tübingen, Germany
4 Max Planck Institut für Entwicklungsbiologie, Spemannstrasse 35, D-72076 Tübingen, Germany

* Corresponding author. E-mail address: anne.spang{at}tuebingen.mpg.de.

Protein trafficking is achieved by a bidirectional vesicle flow between the various compartments of the eukaryotic cell. COPII coated vesicles mediate anterograde protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus whereas retrograde Golgi to ER vesicles use the COPI coat. Inactivation of COPI vesicle formation in conditional sec21 ({gamma}-COP) mutants rapidly blocks transport of certain proteins along the early secretory pathway. We have identified the integral membrane protein Mst27p as a strong suppressor of sec21-3 and ret1-1 mutants. A C-terminal KKXX motif of Mst27p that allows direct binding to the COPI complex is crucial for its suppression ability. Mst27p and its homologue Yar033w (Mst28p) are part of the same complex. Both proteins contain cytoplasmic exposed C-termini that have the ability to interact directly with COPI and COPII coat complexes. Site specific mutations of the COPI binding domain abolished suppression of the sec21 mutants. Our results indicate that overexpression of MST27 provides an increased number of coat binding sites on membranes of the early secretory pathway and thereby promotes vesicle formation. As a consequence, the amount of cargo that can bind COPI might be important for the regulation of the vesicle flow in the early secretory pathway.




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