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Published online 5 March 2001. doi:10.1083/jcb.152.5.935
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© The Rockefeller University Press, 0021-9525/2001//935 $5.00
The Journal of Cell Biology, Volume 152, Number 5, , 2001 935-944

Original Article

Rer1p, a Retrieval Receptor for Endoplasmic Reticulum Membrane Proteins, Is Dynamically Localized to the Golgi Apparatus by Coatomer



Ken Satoa, Miyuki Satoa, and Akihiko Nakanoa

a Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Saitama 351-0198, Japan
Molecular Membrane Biology Lab, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.81-48-462-467981-48-467-9548

satoken{at}postman.riken.go.jp

Rer1p, a yeast Golgi membrane protein, is required for the retrieval of a set of endoplasmic reticulum (ER) membrane proteins. We present the first evidence that Rer1p directly interacts with the transmembrane domain (TMD) of Sec12p which contains a retrieval signal. A green fluorescent protein (GFP) fusion of Rer1p rapidly cycles between the Golgi and the ER. Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole. The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing {alpha} and {gamma} subunits. These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.

Key Words: retrieval • vesicle recycling • Golgi apparatus • coatomer • Saccharomyces cerevisiae

© 2001 The Rockefeller University Press

The online version of this article contains supplemental material.

Abbreviations used in this paper: CCD, charge-coupled device; COP, coat protein; DSP, dithiobis (succinimidyl propionate); GFP, green fluorescent protein; GST, glutathione S-transferase; HA, hemagglutinin; MVB, multivesicular body; TMD, transmembrane domain.


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