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J. Cell Biol., Volume 146, Number 2, July 26, 1999 301-312
Copyright © 1999 by The Rockefeller University Press.

ERG30, a VAP-33–related Protein, Functions in Protein Transport Mediated by COPI Vesicles

Lior Soussana, Darya Burakova, Mathew P. Danielsc, Mira Toister-Achituvb, Amir Poratb, Yossef Yardena, and Zvulun Elazarb
a Department of Biological Regulation, The Weizmann Institute of Science, Rehovot, 76100 Israel
b Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, 76100 Israel
c Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-4036

Correspondence to: Zvulun Elazar, Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, 76100 Israel., bmzevi{at}weizmann.weizmann.ac.il (E-mail), 972-8-9343682 (phone), 972-8-9344112 (fax)

Intracellular transport of newly synthesized and mature proteins via vesicles is controlled by a large group of proteins. Here we describe a ubiquitous rat protein—endoplasmic reticulum (ER) and Golgi 30-kD protein (ERG30)—which shares structural characteristics with VAP-33, a 33-kD protein from Aplysia californica which was shown to interact with the synaptic protein VAMP. The transmembrane topology of the 30-kD ERG30 corresponds to a type II integral membrane protein, whose cytoplasmic NH2 terminus contains a predicted coiled-coil motif. We localized ERG30 to the ER and to pre-Golgi intermediates by biochemical and immunocytochemical methods. Consistent with a role in vesicular transport, anti-ERG30 antibodies specifically inhibit intra-Golgi transport in vitro, leading to significant accumulation of COPI-coated vesicles. It appears that ERG30 functions early in the secretory pathway, probably within the Golgi and between the Golgi and the ER.

Key Words: endoplasmic reticulum, Golgi, coated vesicles, secretion, transport intermediates


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