The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1----6)-beta-D-glucan synthesis and normal cell growth

1990 ◽  
Vol 10 (6) ◽  
pp. 3013-3019
Author(s):  
P Meaden ◽  
K Hill ◽  
J Wagner ◽  
D Slipetz ◽  
S S Sommer ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Cell Growth ◽  
Normal Cell ◽  
Secretory Pathway ◽  
Endoplasmic Reticulum Retention Signal ◽  
Endoplasmic Reticulum Protein ◽  
Glucan Synthesis ◽  
Retention Signal ◽  
Sequential Assembly

Yeast kre mutants define a pathway of cell wall (1----6)-beta-D-glucan synthesis, and mutants in genes KRE5 and KRE6 appear to interact early in such a pathway. We have cloned KRE5, and the sequence predicts the product to be a large, hydrophilic, secretory glycoprotein which contains the COOH-terminal endoplasmic reticulum retention signal, HDEL. Deletion of the KRE5 gene resulted in cells with aberrant morphology and extremely compromised growth. Suppressors to the KRE5 deletions arose at a frequency of 1 in 10(7) to 1 in 10(8) and permitted an analysis of deletions which were found to contain no alkali-insoluble (1----6)-beta-D-glucan. These results indicate a role for (1----6)-beta-D-glucan in normal cell growth and suggest a model for sequential assembly of (1----6)-beta-D-glucan in the yeast secretory pathway.

scholarly journals The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1----6)-beta-D-glucan synthesis and normal cell growth.

1990 ◽  
Vol 10 (6) ◽  
pp. 3013-3019 ◽  
Author(s):  
P Meaden ◽  
K Hill ◽  
J Wagner ◽  
D Slipetz ◽  
S S Sommer ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Cell Growth ◽  
Normal Cell ◽  
Secretory Pathway ◽  
Endoplasmic Reticulum Retention Signal ◽  
Endoplasmic Reticulum Protein ◽  
Glucan Synthesis ◽  
Retention Signal ◽  
Sequential Assembly

Yeast kre mutants define a pathway of cell wall (1----6)-beta-D-glucan synthesis, and mutants in genes KRE5 and KRE6 appear to interact early in such a pathway. We have cloned KRE5, and the sequence predicts the product to be a large, hydrophilic, secretory glycoprotein which contains the COOH-terminal endoplasmic reticulum retention signal, HDEL. Deletion of the KRE5 gene resulted in cells with aberrant morphology and extremely compromised growth. Suppressors to the KRE5 deletions arose at a frequency of 1 in 10(7) to 1 in 10(8) and permitted an analysis of deletions which were found to contain no alkali-insoluble (1----6)-beta-D-glucan. These results indicate a role for (1----6)-beta-D-glucan in normal cell growth and suggest a model for sequential assembly of (1----6)-beta-D-glucan in the yeast secretory pathway.

scholarly journals The Yeast RER2 Gene, Identified by Endoplasmic Reticulum Protein Localization Mutations, Encodescis-Prenyltransferase, a Key Enzyme in Dolichol Synthesis

1999 ◽  
Vol 19 (1) ◽  
pp. 471-483 ◽  
Author(s):  
Miyuki Sato ◽  
Ken Sato ◽  
Shuh-ichi Nishikawa ◽  
Aiko Hirata ◽  
Jun-ichi Kato ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Pathway ◽  
Molecular Mechanisms ◽  
Protein Localization ◽  
Temperature Sensitive ◽  
Large Gene ◽  
Abnormal Accumulation ◽  
Endoplasmic Reticulum Protein ◽  
Key Enzyme ◽  
The Difference

ABSTRACT As an approach to understand the molecular mechanisms of endoplasmic reticulum (ER) protein sorting, we have isolated yeastrer mutants that mislocalize a Sec12-Mfα1p fusion protein from the ER to later compartments of the secretory pathway (S. Nishikawa and A. Nakano, Proc. Natl. Acad. Sci. USA 90:8179–8183, 1993). The temperature-sensitive rer2 mutant mislocalizes different types of ER membrane proteins, suggesting thatRER2 is involved in correct localization of ER proteins in general. The rer2 mutant shows several other characteristic phenotypes: slow growth, defects in N and O glycosylation, sensitivity to hygromycin B, and abnormal accumulation of membranes, including the ER and the Golgi membranes.RER2 and SRT1, a gene whose overexpression suppresses rer2, encode novel proteins similar to each other, and their double disruption is lethal.RER2 homologues are found not only in eukaryotes but also in many prokaryote species and thus constitute a large gene family which has been well conserved during evolution. Taking a hint from the phenotype of newly established mutants of the Rer2p homologue of Escherichia coli, we discovered that therer2 mutant is deficient in the activity ofcis-prenyltransferase, a key enzyme of dolichol synthesis. This and other lines of evidence let us conclude that members of theRER2 family of genes encodecis-prenyltransferase itself. The difference in phenotypes between the rer2 mutant and previously obtained glycosylation mutants suggests a novel, as-yet-unknown role of dolichol.

scholarly journals Defective Human Ether-à-go-go-related Gene Trafficking Linked to an Endoplasmic Reticulum Retention Signal in the C Terminus

2002 ◽  
Vol 277 (30) ◽  
pp. 27442-27448 ◽  
Author(s):  
Sabina Kupershmidt ◽  
Tao Yang ◽  
Siprachanh Chanthaphaychith ◽  
Zhiqing Wang ◽  
Jeffrey A. Towbin ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Related Gene ◽  
Endoplasmic Reticulum Retention ◽  
C Terminus ◽  
Endoplasmic Reticulum Retention Signal ◽  
Retention Signal

scholarly journals The medial-Golgi Ion Pump Pmr1 Supplies the Yeast Secretory Pathway with Ca2+ and Mn2+ Required for Glycosylation, Sorting, and Endoplasmic Reticulum-Associated Protein Degradation

1998 ◽  
Vol 9 (5) ◽  
pp. 1149-1162 ◽  
Author(s):  
Gabriele Dürr ◽  
Jochen Strayle ◽  
Richard Plemper ◽  
Saskia Elbs ◽  
Saskia K. Klee ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
Intracellular Transport ◽  
Secretory Pathway ◽  
Protein Glycosylation ◽  
Carboxypeptidase Y ◽  
Dual Function ◽  
Ion Pump ◽  
Endoplasmic Reticulum Protein ◽  
Sorting Receptor

The yeast Ca2+ adenosine triphosphatase Pmr1, located in medial-Golgi, has been implicated in intracellular transport of Ca2+ and Mn2+ ions. We show here that addition of Mn2+ greatly alleviates defects ofpmr1 mutants in N-linked and O-linked protein glycosylation. In contrast, accurate sorting of carboxypeptidase Y (CpY) to the vacuole requires a sufficient supply of intralumenal Ca2+. Most remarkably, pmr1 mutants are also unable to degrade CpY*, a misfolded soluble endoplasmic reticulum protein, and display phenotypes similar to mutants defective in the stress response to malfolded endoplasmic reticulum proteins. Growth inhibition of pmr1 mutants on Ca2+-deficient media is overcome by expression of other Ca2+ pumps, including a SERCA-type Ca2+ adenosine triphosphatase from rabbit, or by Vps10, a sorting receptor guiding non-native luminal proteins to the vacuole. Our analysis corroborates the dual function of Pmr1 in Ca2+ and Mn2+ transport and establishes a novel role of this secretory pathway pump in endoplasmic reticulum-associated processes.

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