The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae

被引：96

作者：

Springer, S

Chen, E

Duden, R

Marzioch, M

Rowley, A

Hamamoto, S

Merchant, S

Schekman, R

机构：

[1] Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[3] Univ Cambridge, Cambridge Inst Med Res, Dept Clin Biochem, Cambridge CB2 2XY, England

[4] Glaxo Wellcome Res & Dev Ltd, Cell Biol Unit, Stevenage SG1 2NY, Herts, England

[5] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 08期

基金：

英国惠康基金;

关键词：

D O I：

10.1073/pnas.070044097

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

To investigate the factors involved in the sorting of cargo proteins into COPII endoplasmic reticulum (ER) to Golgi apparatus transport vesicles, we have created a strain of S. cerevisiae (p24 Delta 8) that lacks all eight members of the p24 family of transmembrane proteins (Emp24p, Erv25p, and Erp1p to Erp6p). The p24 proteins have been implicated in COPI and COPII vesicle formation, cargo protein sorting, and regulation of vesicular transport in eukaryotic cells. We find that p24 Delta 8 cells grow identically to wild type and show delays of invertase and Gas1p ER-to-Golgi transport identical to those seen in a single Delta emp24 deletion strain. Thus, p24 proteins do not have an essential function in the secretory pathway. instead, they may serve as quality control factors to restrict the entry of proteins into COPII vesicles.

引用

页码：4034 / 4039

页数：6

共 44 条

[11] THE VACUOLAR H+-ATPASE OF SACCHAROMYCES-CEREVISIAE IS REQUIRED FOR EFFICIENT COPPER DETOXIFICATION, MITOCHONDRIAL-FUNCTION, AND IRON-METABOLISM [J].