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

Jesse C. Hay; Daniel S. Chao; Christin S. Kuo; Richard H. Scheller

doi:10.1016/S0092-8674(00)80191-9

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

Jesse C. Hay
, Daniel S. Chao
, Christin S. Kuo
, Richard H. Scheller

Stanford University

Research output: Contribution to journal › Article › peer-review

189 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	149-158
Number of pages	10
Journal	Cell
Volume	89
Issue number	1
DOIs	https://doi.org/10.1016/S0092-8674(00)80191-9
State	Published - Apr 4 1997

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title = "Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells",

abstract = "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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T1 - Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells

AU - Hay, Jesse C.

AU - Chao, Daniel S.

AU - Kuo, Christin S.

AU - Scheller, Richard H.

PY - 1997/4/4

Y1 - 1997/4/4

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0030890594

U2 - 10.1016/S0092-8674(00)80191-9

DO - 10.1016/S0092-8674(00)80191-9

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VL - 89

SP - 149

EP - 158

JO - Cell

JF - Cell

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ER -

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

Abstract

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