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    Cell. 1997 Apr 4;89(1):149-58.

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

    Hay JC, Chao DS, Kuo CS, Scheller RH.

    Department of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5428, USA.

    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.

    PMID: 9094723 [PubMed - indexed for MEDLINE]

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