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

First Author  Hay JC Year  1997
Journal  Cell Volume  89
Issue  1 Pages  149-58
PubMed ID  9094723 Mgi Jnum  J:46012
Mgi Id  MGI:1196819 Doi  10.1016/s0092-8674(00)80191-9
Citation  Hay JC, et al. (1997) Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell 89(1):149-58
abstractText  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.
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