Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells

Jesse C. Hay, Daniel S. Chao, Christin S. Kuo, Richard H. Scheller

Research output: Contribution to journalArticlepeer-review

Abstract

The proposed cis-Golgi vesicle receptor syntaxin 5 was found in a complex with Golgi-associated SNARE of 28 kDa (GOS-28), rbet1, rsly1, and two novel proteins characterized herein: rat sec22b and membrin, both cytoplasmically oriented integral membrane proteins. The complex appears to recapitulate vesicle docking interactions of proteins originating from distinct compartments, since syntaxin 5, rbet1, and GOS-28 localize to Golgi membranes, whereas mouse sec22b and membrin accumulate in the endoplasmic reticulum. Protein interactions in the complex are dramatically rearranged by N-ethylmaleimide-sensitive factor. The complex consists of two or more subcomplexes with some members (rat sec22b and syntaxin 5) in common and others (rbet1 and GOS-28) mutually exclusively associated. We propose that these protein interactions determine vesicle docking/fusion fidelity between the endoplasmic reticulum and Golgi.

Original languageEnglish
Pages (from-to)149-158
Number of pages10
JournalCell
Volume89
Issue number1
DOIs
StatePublished - Apr 4 1997

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