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.
Mesh Terms:
Animals, Biological Transport, COS Cells, Carrier Proteins, Detergents, Endoplasmic Reticulum, Epitopes, Gene Expression, Golgi Apparatus, Mammals, Membrane Proteins, Mice, Molecular Sequence Data, N-Ethylmaleimide-Sensitive Proteins, Nerve Tissue Proteins, Neurons, Qa-SNARE Proteins, Qb-SNARE Proteins, Qc-SNARE Proteins, R-SNARE Proteins, Rabbits, Rats, Rats, Sprague-Dawley, Sequence Homology, Amino Acid, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins, Subcellular Fractions, Synaptic Vesicles, Vesicular Transport Proteins
Cell
Date: Apr. 04, 1997
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