spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Martinez, P.
Right arrow Articles by Ljungdahl, P. O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martinez, P.
Right arrow Articles by Ljungdahl, P. O.

Journal of Cell Science, Vol 113, Issue 23 4351-4362, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

The SHR3 homologue from S. pombe demonstrates a conserved function of ER packaging chaperones

P Martinez and PO Ljungdahl
Ludwig Institute for Cancer Research, Box 240, S-17177 Stockholm, Sweden. plju@licr.ki.se.

In Saccharomyces cerevisiae cells lacking SHR3, amino acid permeases do not enter into COPII transport vesicles and specifically accumulate in the membrane of the endoplasmic reticulum. Shr3p functions as a packaging chaperone to prime transport vesicle formation in the proximity of amino acid permeases. A genetic screen was developed that enabled the Schizosaccharomyces pombe SHR3 functional homologue, designated psh3(+) (pombe SHR3), to be cloned. The psh3(+) gene encodes a protein of 215 amino acids, which shares a high degree of structural and functional similarity with Shr3p. The heterologous expression of psh3(+) complements many, but not all, shr3 null mutant phenotypes in S. cerevisiae in a temperature-dependent manner. Psh3p is localised to the endoplasmic reticulum of S. pombe cells, and strains lacking the psh3(+ )gene exhibit decreased rates of amino acid uptake due to reduced levels of functional permeases in the plasma membrane. No packaging chaperones, or proteins exhibiting homology with packaging chaperones, have so far been identified in other eukayotic organisms. The findings reported here are the first to establish that specific packaging chaperones exist in divergent organisms, and demonstrate a conserved function of packaging chaperones in facilitating the export of large polytopic membrane proteins from the endoplasmic reticulum.


This article has been cited by other articles:


Home page
 Mol. Pharmacol.Home page
D. Kowalski, L. Pendyala, B. Daignan-Fornier, S. B. Howell, and R.-Y. Huang
Dysregulation of Purine Nucleotide Biosynthesis Pathways Modulates Cisplatin Cytotoxicity in Saccharomyces cerevisiae
Mol. Pharmacol., October 1, 2008; 74(4): 1092 - 1100.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
C. Andreasson, S. Heessen, and P. O. Ljungdahl
Regulation of transcription factor latency by receptor-activated proteolysis.
Genes & Dev., June 15, 2006; 20(12): 1563 - 1568.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
P. Martinez and P. O. Ljungdahl
Divergence of Stp1 and Stp2 Transcription Factors in Candida albicans Places Virulence Factors Required for Proper Nutrient Acquisition under Amino Acid Control
Mol. Cell. Biol., November 1, 2005; 25(21): 9435 - 9446.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
J. Kota and P. O. Ljungdahl
Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER
J. Cell Biol., January 3, 2005; 168(1): 79 - 88.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2000