The yeast homolog of H &lt; beta &gt; 58, a mouse gene essential for embryogenesis, performs a role in the delivery of proteins to the vacuole.

Bachhawat, Anand K.; Suhan, Joseph; Jones, Elizabeth W.

doi:10.1101/gad.8.12.1379

Cited by 23 publications

(26 citation statements)

References 51 publications

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“…Therefore, a domain swap experiment was performed in which the C-terminal third of Vps26p was replaced with the homologous region of H␤58, the mouse homolog. This Vps26p-H␤58 hybrid has been shown previously to fully complement the CPY sorting defect in a vps26⌬ cell (Bachhawat et al, 1994). We also found this to be the case; however, to our surprise we found that the presence of an HA tag in the N-terminal half of the protein rendered the Vps26p-HA-H␤58 hybrid completely nonfunctional ( Figure 4B).…”

Section: Figurementioning

confidence: 39%

“…Replacing the carboxy terminus of Vps26p with the homologous region of the mouse homolog H␤58 resulted in a hybrid molecule that was fully functional. This hybrid construct was also generated by Jones and colleagues and was reported to be fully functional in its ability to complement CPY sorting in a vps26 mutant (Bachhawat et al, 1994). To facilitate detection of the hybrid construct a HA epitope-tagged construct, in which a triple HA tag was inserted between residues 76/77, was used as the basis for this hybrid construct.…”

Section: Role Of Vps26p In Retromer Functionmentioning

confidence: 98%

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Vps26p, a Component of Retromer, Directs the Interactions of Vps35p in Endosome-to-Golgi Retrieval

Reddy

Seaman

2001

MBoC

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Endosome-to-Golgi retrieval of the carboxypeptidase Y receptor Vps10p is mediated by a recently discovered membrane coat complex termed retromer. Retromer comprises five conserved proteins: Vps35p, Vps29p, Vps5p, Vps17p, and Vps26p. Vps35p recognizes cargo molecules such as Vps10p and interacts strongly with Vps29p. Vps5p forms a subcomplex with Vps17p and has been proposed to play a structural role by self-assembling into large multimeric structures. The function of Vps26p is currently unknown. We have investigated the role that Vps26p plays in retromer-mediated endosome-to-Golgi transport by analyzing dominant negative alleles of Vps26p. These mutants have identified a crucial region of Vps26p that plays an important role in its function. Functional domains of Vps26p have been investigated by the creation of yeast-mouse hybrid molecules in which domains of Vps26p have been replaced by the similar domain in the protein encoded by the mouse VPS26 gene, Hbeta58. These domain swap experiments have shown that Vps26p promotes the interactions between the cargo-selective component Vps35p and the structural components Vps5p/Vps17p.

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Section: Figurementioning

confidence: 39%

Section: Role Of Vps26p In Retromer Functionmentioning

confidence: 98%

Vps26p, a Component of Retromer, Directs the Interactions of Vps35p in Endosome-to-Golgi Retrieval

Reddy

Seaman

2001

MBoC

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“…The plasmids used in this study are listed in Table 1. pSN269 is pBluescript KS ϩ (Stratagene, La Jolla, Calif.) with a 2.0-kbp XhoI-XbaI PCR-generated insert consisting of the entire PEP8 gene (2) in which the PEP8 open reading frame was precisely replaced with the LEU2 gene. pSN273 was constructed by subcloning the 3.0-kbp SacI-XhoI fragment from pTS17 (1) into the SacI-XhoI sites of pBluescript KS ϩ .…”

Section: Methodsmentioning

confidence: 99%

The Newly Identified Yeast GRD Genes Are Required for Retention of Late-Golgi Membrane Proteins

Nothwehr

Bryant

Stevens

1996

Molecular and Cellular Biology

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Processing of A-ALP, a late-Golgi membrane protein constructed by fusing the cytosolic domain of dipeptidyl aminopeptidase A to the transmembrane and lumenal domains of alkaline phosphatase (ALP), serves as a convenient assay for loss of retention of late-Golgi membrane proteins in Saccharomyces cerevisiae. In this study, a large group of novel grd (for Golgi retention defective) yeast mutants, representing 18 complementation groups, were identified on the basis of their mislocalization of A-ALP to the vacuole, where it was proteolytically processed and thus became enzymatically activated. All of the grd mutants exhibited significant mislocalization of A-ALP, as measured by determining the kinetics of A-ALP processing and by analyzing its localization by indirect immunofluorescence microscopy. The mutants were evaluated in a variety of other phenotypic tests relevant to yeast Golgi function, including processing of the ␣-factor mating pheromone, sorting of the vacuolar hydrolase carboxypeptidase Y, and retention of an early-Golgi membrane protein.Mutants from three grd complementation groups also failed to retain an early-Golgi membrane protein, suggesting that these mutations may have more global effects on Golgi retention and function. However, the majority of the grd mutants appeared to be defective specifically for the retention of several late-Golgi membrane proteins. A subset of the grd mutants appeared defective only in retention of A-ALP and not other late-Golgi membrane proteins. The grd mutants define a new set of genes required for Golgi membrane protein retention in S. cerevisiae.

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“…SNX1 binds to the cytoplasmic tail of the epidermal growth factorreceptor (EGFR) (17) where it may play a role in endosome to lysosome trafficking. The Vps26p protein (18) is homologous to mouse H␤58 which is essential for completing embryogenesis (19).…”

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confidence: 99%

Human Homologues of Yeast Vacuolar Protein Sorting 29 and 35

Edgar

Polak

2000

Biochemical and Biophysical Research Communications

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The yeast homolog of H < beta > 58, a mouse gene essential for embryogenesis, performs a role in the delivery of proteins to the vacuole.

Abstract: The highly conserved and ubiquitously expressed mouse gene H<1~>58, identified through insertional mutagenesis, has been shown to be essential for early postimplantation development in mouse, but the mechanism by which it acts is unknown (

Cited by 23 publications

References 51 publications

Vps26p, a Component of Retromer, Directs the Interactions of Vps35p in Endosome-to-Golgi Retrieval

Vps26p, a Component of Retromer, Directs the Interactions of Vps35p in Endosome-to-Golgi Retrieval

The Newly Identified Yeast GRD Genes Are Required for Retention of Late-Golgi Membrane Proteins

Human Homologues of Yeast Vacuolar Protein Sorting 29 and 35

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