» Articles » PMID: 2542798

Vesicular Transport Between the Endoplasmic Reticulum and the Golgi Stack Requires the NEM-sensitive Fusion Protein

Overview
Journal Nature
Specialty Science
Date 1989 Jun 1
PMID 2542798
Citations 94
Authors
Affiliations
Soon will be listed here.
Abstract

An N-ethylmaleimide-sensitive fusion protein (NSF) has been purified on the basis of its ability to catalyse vesicular transport within the Golgi stack. We report here that this same protein is required for transport from the endoplasmic reticulum to the Golgi stack in semi-intact cells. This transport process is inhibited by a monoclonal antibody against NSF. Furthermore, pretreatment of semi-intact cells with N-ethylmaleimide, a sulphydryl alkylating reagent, inhibits transport. Addition of highly purified NSF largely restores transport from endoplasmic reticulum to Golgi. These results suggest that NSF is a general component of the transport machinery required for membrane fusion at multiple stages of the secretory pathway.

Citing Articles

ER exit in physiology and disease.

Robinson C, Duggan A, Forrester A Front Mol Biosci. 2024; 11:1352970.

PMID: 38314136 PMC: 10835805. DOI: 10.3389/fmolb.2024.1352970.


LRRK2 along the Golgi and lysosome connection: a jamming situation.

Piccoli G, Volta M Biochem Soc Trans. 2021; 49(5):2063-2072.

PMID: 34495322 PMC: 8589420. DOI: 10.1042/BST20201146.


LRRK2 and the Endolysosomal System in Parkinson's Disease.

Erb M, Moore D J Parkinsons Dis. 2020; 10(4):1271-1291.

PMID: 33044192 PMC: 7677880. DOI: 10.3233/JPD-202138.


Porcine Epidemic Diarrhea Virus ORF3 Protein Is Transported through the Exocytic Pathway.

Si F, Chen B, Hu X, Yu R, Dong S, Wang R J Virol. 2020; 94(17).

PMID: 32554695 PMC: 7431808. DOI: 10.1128/JVI.00808-20.


A family of PIKFYVE inhibitors with therapeutic potential against autophagy-dependent cancer cells disrupt multiple events in lysosome homeostasis.

Sharma G, Guardia C, Roy A, Vassilev A, Saric A, Griner L Autophagy. 2019; 15(10):1694-1718.

PMID: 30806145 PMC: 6735543. DOI: 10.1080/15548627.2019.1586257.