Protein Interactions Regulating Vesicle Transport between the Endoplasmic Reticulum and Golgi Apparatus in Mammalian Cells

• Published in: Cell Vol. 89; no. 1; pp. 149 - 158
• Main Authors: Hay, Jesse C, Chao, Daniel S, Kuo, Christin S, Scheller, Richard H
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04.04.1997
• Subjects: Animals; Biological Transport - physiology; Carrier Proteins - physiology; COS Cells - physiology; Detergents; Endoplasmic Reticulum - chemistry; Endoplasmic Reticulum - metabolism; Epitopes - analysis; Gene Expression - physiology; Golgi Apparatus - chemistry; Golgi Apparatus - metabolism; Mammals; Membrane Proteins - analysis; Membrane Proteins - genetics; Membrane Proteins - isolation & purification; Membrane Proteins - physiology; Mice; Molecular Sequence Data; N-Ethylmaleimide-Sensitive Proteins; Nerve Tissue Proteins - analysis; Nerve Tissue Proteins - isolation & purification; Neurons - cytology; Neurons - metabolism; 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 - chemistry; Synaptic Vesicles - chemistry; Synaptic Vesicles - metabolism; Vesicular Transport Proteins
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(00)80191-9

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.