Identification of a gene required for membrane protein retention in the early secretory pathway

The yeast SEC12 gene product (Sec12p) is an integral membrane protein required for the protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus. Although this protein is almost exclusively localized in the ER, a significant fraction of Sec12p is modified by an enzyme that resides...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 90; no. 17; pp. 8179 - 8183
Main Authors Nishikawa, S, Nakano, A
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 01.09.1993
National Acad Sciences
National Academy of Sciences
Subjects
Online AccessGet full text
ISSN0027-8424
1091-6490
1091-6490
DOI10.1073/pnas.90.17.8179

Cover

More Information
Summary:The yeast SEC12 gene product (Sec12p) is an integral membrane protein required for the protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus. Although this protein is almost exclusively localized in the ER, a significant fraction of Sec12p is modified by an enzyme that resides in the early compartment of the Golgi apparatus, suggesting that Sec12p is cycling between the ER and the early Golgi. We have taken a genetic approach to investigate the retention mechanism of Sec12p. Analysis of mutants that are defective in the retention of the Sec12-Mf alpha 1 fusion protein in the early secretory compartments has identified a gene, RER1. A recessive mutation in RER1 causes mislocalization of the authentic Sec12p as well as two different Sec12 fusion proteins to the late Golgi apparatus and even to the cell surface. However, the rer1 mutant is not defective in the retention of an Er-resident soluble protein, BiP, suggesting that soluble and membrane proteins are retained in the ER by distinct mechanisms
Bibliography:F60
F30
9431095
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 14
ObjectType-Article-2
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0027-8424
1091-6490
1091-6490
DOI:10.1073/pnas.90.17.8179