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Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells.
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.[1]References
- Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Hay, J.C., Chao, D.S., Kuo, C.S., Scheller, R.H. Cell (1997) [Pubmed]
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