Characterization of the ORF YBR264c in Saccharomyces cerevisiae, which encodes a new yeast Ypt that is degraded by a proteasome-dependent mechanism

Louvet, Olivier; Roumanie, Olivier; Barthe, Christophe; Peypouquet, Marie-France; Schaeffer, Jacques; Doignon, François; Crouzet, Marc

doi:10.1007/s004380050001

Cited by 11 publications

(11 citation statements)

References 68 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of a PEST sequence in a yeast small G protein has already been reported for the Ypt10 Rab protein. It has been shown that the Ypt10p PEST sequence played a role in protein stability, and that Ypt10p degradation is dependent on proteasome activity [32]. In a similar way, we suppose that the PEST sequence is implicated in vivo in regulating Rho5 protein abundance.…”

Section: Resultsmentioning

confidence: 55%

Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae

et al. 2001

View full text Add to dashboard Cite

Rho proteins are down-regulated in vivo by specific GTPase activating proteins (RhoGAP). We have functionally studied three Saccharomyces cerevisiae putative RhoGAP. By first identifying Rho partners with a systematic two-hybrid approach and then using an in vitro assay, we have demonstrated that the Bag7 protein stimulated the GTPase activity of the Rho1 protein, Lrg1p acted on the Cdc42 and Rho2 GTPases and we showed that Rgd2p has a GAP activity on both Cdc42p and Rho5p. In addition, we brought the first evidence for the existence of a sixth functional Rho in yeast, the Cdc42/Rac-like GTPase Rho5. ß

show abstract

Section: Resultsmentioning

confidence: 55%

Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae

et al. 2001

View full text Add to dashboard Cite

show abstract

“…These data suggest that the tagged Ypt7p can function equivalently to the untagged protein. No functions have been described for the Rab protein Ypt10p or Ypt11p, and mutants with deletions of the genes encoding either protein have no apparent phenotype; however, Ypt10p is known to be deleterious to cell growth when overexpressed (38). We asked whether the overexpression of GFP-YPT10 would result in similar growth inhibition.…”

Section: Resultsmentioning

confidence: 98%

“…Ypt10p is a Rab protein whose overexpression is growth inhibitory with possible defects in vesicular traffic (38) but otherwise mysterious; its localization has not been determined. Our bioinformatics analysis did not reveal Ypt10p to be a member of a large subclass of Rab proteins.…”

Section: Vol 26 2006 Evolutionary Conservation Of Rab Localization mentioning

confidence: 99%

“…The existence of the two yeast Rabs Ypt10p and Ypt11p was revealed only upon the sequencing of the yeast genome, and these ORFs remain functionally uncharacterized. Little is known about Ypt10p other than the observation of possible defects in vesicular traffic upon the overexpression of Ypt10p (38). To date, no function or localization has been assigned to Ypt11p.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Bioinformatic and Comparative Localization of Rab Proteins Reveals Functional Insights into the Uncharacterized GTPases Ypt10p and Ypt11p

Frei

Rahl

Nussbaum

et al. 2006

Molecular and Cellular Biology

View full text Add to dashboard Cite

A striking characteristic of a Rab protein is its steady-state localization to the cytosolic surface of a particular subcellular membrane. In this study, we have undertaken a combined bioinformatic and experimental approach to examine the evolutionary conservation of Rab protein localization. A comprehensive primary sequence classification shows that 10 out of the 11 Rab proteins identified in the yeast (Saccharomyces cerevisiae) genome can be grouped within a major subclass, each comprising multiple Rab orthologs from diverse species. We compared the locations of individual yeast Rab proteins with their localizations following ectopic expression in mammalian cells. Our results suggest that green fluorescent protein-tagged Rab proteins maintain localizations across large evolutionary distances and that the major known player in the Rab localization pathway, mammalian Rab-GDI, is able to function in yeast. These findings enable us to provide insight into novel gene functions and classify the uncharacterized Rab proteins Ypt10p (YBR264C) as being involved in endocytic function and Ypt11p (YNL304W) as being localized to the endoplasmic reticulum, where we demonstrate it is required for organelle inheritance.All eukaryotic cells are compartmentalized into distinct membrane-bound organelles and require tightly regulated transport of proteins and lipids between these compartments. Members of the Rab family of small GTPases are major regulators of protein and lipid traffic in the secretory and endocytic pathways (46,65). The action of Rab proteins in membrane transport was discovered with the identification of the SEC4 and YPT1 genes in yeast (Saccharomyces cerevisiae) (51, 52) and related proteins, termed Rab proteins, from mammals (10). Rab proteins comprise the most numerous subfamily of the Ras superfamily, and many are functionally uncharacterized. It is not clear whether Rab proteins regulate events that take place in the donor compartment, the vesicle or transport carrier, the acceptor compartment, or multiple locations. Also not known is whether a function(s) can be described for Rab proteins in general or whether this must be considered on a case-by-case basis. However, it is clear that Rab proteins are essential for eukaryotic cells and absolutely required for the function of all organelles connected by SNARE-mediated membrane traffic.With the completion of eukaryotic genome sequencing projects, there have been efforts to catalog the numbers of GTPase superfamily proteins. Membrane traffic in higher eukaryotes connects multiple compartments, and one reflection of this complexity may be the finding that humans have at least 60 different Rab family members (24,55,57). Other eukaryotes have fewer Rab proteins; Caenorhabditis elegans has 29 family members, Drosophila melanogaster has 26 members, and the yeast Saccharomyces cerevisiae has 11 members. As a model system, the 11 Rab proteins of the single-celled eukaryotic microbe S. cerevisiae can be considered the most minimal "membrome" (24), as other single-celle...

show abstract

“…A balanced ratio between the many actors in the secretory pathway (6) may therefore be critical for normal growth. In fact, toxic effects have been observed upon overexpression of YPT10 in S. cerevisiae, apparently due to alteration of structures in the Golgi apparatus (21). On the other hand, overproduction of wild-type Sec4p in C. albicans did not affect growth, while mutant forms behave as dominant-negative alleles (6,14,22).…”

Section: Discussionmentioning

confidence: 99%

The Genes of Two G-Proteins Involved in Protein Transport in Pichia pastoris

Huynh

Vad

Kristensen

et al. 2001

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Characterization of the ORF YBR264c in Saccharomyces cerevisiae, which encodes a new yeast Ypt that is degraded by a proteasome-dependent mechanism

Cited by 11 publications

References 68 publications

Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae

Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae

Bioinformatic and Comparative Localization of Rab Proteins Reveals Functional Insights into the Uncharacterized GTPases Ypt10p and Ypt11p

The Genes of Two G-Proteins Involved in Protein Transport in Pichia pastoris

Contact Info

Product

Resources

About