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

doi:10.1083/jcb.152.5.935

Published online 5 March 2001. doi:10.1083/jcb.152.5.935

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© The Rockefeller University Press, 0021-9525/2001/3/935/ $5.00
The Journal of Cell Biology, Volume 152, Number 5, March 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 Sato^a, Miyuki Sato^a, and Akihiko Nakano^a
^a Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Saitama 351-0198, Japan

Correspondence to: Ken Sato, Molecular Membrane Biology Lab, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Tel:81-48-467-9548 Fax:81-48-462-4679 E-mail:satoken{at}postman.riken.go.jp.

Rer1p, a yeast Golgi membrane protein, is required for the retrievalof a set of endoplasmic reticulum (ER) membrane proteins. Wepresent the first evidence that Rer1p directly interacts withthe transmembrane domain (TMD) of Sec12p which contains a retrievalsignal. A green fluorescent protein (GFP) fusion of Rer1p rapidlycycles between the Golgi and the ER. Either a lesion of coatomeror deletion of the COOH-terminal tail of Rer1p causes its mislocalizationto the vacuole. The COOH-terminal Rer1p tail interacts in vitrowith a coatomer complex containing ${alpha}$ and ${gamma}$ subunits. These findingsnot only give the proof that Rer1p is a novel type of retrievalreceptor recognizing the TMD in the Golgi but also indicatethat coatomer actively regulates the function and localizationof Rer1p.

Key Words: retrieval, vesicle recycling, Golgi apparatus, coatomer, Saccharomycescerevisiae

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