Human Homologues of Yeast Vacuolar Protein Sorting 29 and 35

Edgar, Alasdair J.; Polak, Julia M.

doi:10.1006/bbrc.2000.3727

Cited by 38 publications

(31 citation statements)

References 34 publications

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“…These vps proteins are also found in humans. The human homologues hVps26, hVps29 and hVps35 are assembled into multimeric complexes that also comprise SNX1 and SNX2, equivalent to yeast Vps5p and Vps17p, respectively (Haft et al, 2000;Edgar & Polak, 2000). These observations support the notion that the retromer complex is conserved and serves related functions in protein trafficking, thereby recycling receptors in Sch.…”

Section: Discussionsupporting

confidence: 65%

Vacuolar protein sorting receptor in Schizosaccharomyces pombe

et al. 2006

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The mechanism by which soluble proteins, such as carboxypeptidase Y, reach the vacuole in Saccharomyces cerevisiae is very similar to the mechanism of lysosomal protein sorting in mammalian cells. Vps10p is a receptor for transport of soluble vacuolar proteins in S. cerevisiae. vps10+ , a gene encoding a homologue of S. cerevisiae PEP1/VPS10, has been identified and deleted from the fission yeast Schizosaccharomyces pombe.

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Section: Discussionsupporting

confidence: 65%

Vacuolar protein sorting receptor in Schizosaccharomyces pombe

et al. 2006

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“…This suggests that the UPR becomes induced in our experiments, and that the ATF6 pathway limits viral replication. NS5A-interacting proteins that modulate HCV replication include VAP-A/B and VPS35, which function in vesicular trafficking (27)(28)(29)(30). VAPA can bind to NS5B as well as hypophosphorylated NS5A and has been proposed to serve as a scaffold for the replication complex within lipid microdomains (31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

Cellular cofactors affecting hepatitis C virus infection and replication

Randall

Panis²,

Cooper

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

496

454

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Recently identified hepatitis C virus (HCV) isolates that are infectious in cell culture provide a genetic system to evaluate the significance of virus-host interactions for HCV replication. We have completed a systematic RNAi screen wherein siRNAs were designed that target 62 host genes encoding proteins that physically interact with HCV RNA or proteins or belong to cellular pathways thought to modulate HCV infection. This includes 10 host proteins that we identify in this study to bind HCV NS5A. siRNAs that target 26 of these host genes alter infectious HCV production >3-fold. Included in this set of 26 were siRNAs that target Dicer, a principal component of the RNAi silencing pathway. Contrary to the hypothesis that RNAi is an antiviral pathway in mammals, as has been reported for subgenomic HCV replicons, siRNAs that target Dicer inhibited HCV replication. Furthermore, siRNAs that target several other components of the RNAi pathway also inhibit HCV replication. MicroRNA profiling of human liver, human hepatoma Huh-7.5 cells, and Huh-7.5 cells that harbor replicating HCV demonstrated that miR-122 is the predominant microRNA in each environment. miR-122 has been previously implicated in positively regulating the replication of HCV genotype 1 replicons. We find that 2-O-methyl antisense oligonucleotide depletion of miR-122 also inhibits HCV genotype 2a replication and infectious virus production. Our data define 26 host genes that modulate HCV infection and indicate that the requirement for functional RNAi for HCV replication is dominant over any antiviral activity this pathway may exert against HCV.antivirals ͉ miR-122 ͉ RNAi ͉ HCVcc-siRNA H epatitis C virus (HCV) has a notable ability to establish persistent infections in Ϸ70% of cases, resulting in 130 million chronically infected people throughout the world (1). This prevalence has spurred considerable interest in the study of HCV-host interactions, on both cellular and molecular levels. The inability to grow HCV in cell culture led some groups to focus on the identification of cellular proteins that interact with individual HCV proteins or RNA elements, resulting in the accumulation of a large number of putative HCV-host interactions. Unfortunately, the significance of most of these with respect to the HCV life cycle is currently unknown (reviewed in ref.2). Over the past 6 years, cell culture systems have been developed that enable the characterization of HCV replication and entry (3-6). This effort recently culminated in the development of cell culture systems that reproduce the entire viral life cycle (7-9). A number of virus-host interactions have been characterized by using these experimental systems. For example, CD81 has been demonstrated to play a role in HCV entry (10-12).Sequence-specific gene silencing of RNAi is ideal for assessing the genetic phenotypes associated with virus-host interactions. We have previously shown that siRNAs are highly effective at silencing either host or viral RNAs in cells that contain replicating HCV, demonstrating th...

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“…Analysis of zd163 genomic DNA revealed a 148 bp deletion that removes part of intron 7 and exon 8 and probably eliminates most or all function. vps-35 is predicted to encode an 821 amino acid protein that is a homolog of yeast and mammalian VPS35 (Paravicini et al, 1992;Edgar and Polak, 2000;Zhang et al, 2000).…”

Section: Vps-35 Mutants Have Ap Polarity Defects Like Wnt and Frizzlementioning

confidence: 99%

Wnt signaling establishes anteroposterior neuronal polarity and requires retromer inC. elegans

2006

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Secreted Wnt proteins influence neural connectivity by regulating axon guidance, dendritic morphogenesis and synapse formation. We report a new role for Wnt and Frizzled proteins in establishing the anteroposterior polarity of the mechanosensory neurons ALM and PLM in C. elegans. Disruption of Wnt signaling leads to a complete inversion of ALM and PLM polarity: the anterior process adopts the length, branching pattern and synaptic properties of the wild-type posterior process, and vice versa. Different but overlapping sets of Wnt proteins regulate neuronal polarity in different body regions. Wnts act directly on PLM via the Frizzled LIN-17. In addition, we show that they are needed for axon branching and anteriorly directed axon growth. We also find that the retromer, a conserved protein complex that mediates transcytosis and endosome-to-Golgi protein trafficking, plays a key role in Wnt signaling. Deletion mutations of retromer subunits cause ALM and PLM polarity, and other Wnt-related defects. We show that retromer protein VPS-35 is required in Wnt-expressing cells and propose that retromer activity is needed to generate a fully active Wnt signal.

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Human Homologues of Yeast Vacuolar Protein Sorting 29 and 35

Cited by 38 publications

References 34 publications

Vacuolar protein sorting receptor in Schizosaccharomyces pombe

Vacuolar protein sorting receptor in Schizosaccharomyces pombe

Cellular cofactors affecting hepatitis C virus infection and replication

Wnt signaling establishes anteroposterior neuronal polarity and requires retromer inC. elegans

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