A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation.

Robinson, J S; Graham, Todd R.; Emr, Scott D.

doi:10.1128/mcb.11.12.5813

Cited by 77 publications

(67 citation statements)

References 33 publications

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“…To test the significance of the putative zinc-binding motifs of VACI, we mutated codons encoding cysteine or histidine to serine in each of the predicted zinc-coordinating motifs and assayed the effect of these mutations on CPY sorting (Figure 2). Relatively conservative changes of cysteine/histidine to serine were made because serine is able to coordinate zinc poorly and an analogous mutation in the RING motif of vpsl8 resulted in a temperature-conditional Vps-phenotype (Robinson et al, 1991). In addition, we also made several mutations in codons encoding other conserved residues (W212A, K234D, and G241A) of the carboxylterminal RING motif.…”

Section: Resultsmentioning

confidence: 99%

A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.

Burd

Peterson

Cowles

et al. 1997

MBoC

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148

168

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Section: Resultsmentioning

confidence: 99%

A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.

Burd

Peterson

Cowles

et al. 1997

MBoC

Self Cite

148

168

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“…Given that C-Vps in yeast acts as a tethering factor in vesicle fusion 33 , and that mutations in Drosophila homologues of C-Vps subunits induce autophagosome maturation defects 25,26,34,35 , we initially assessed the effects of UVRAG on autophagosome maturation by measuring the colocalization efficiency of GFP-LC3-labelled autophagosomes with LAMP1-stained late endosomes/lysosomes (Fig. 4a).…”

Section: Autophagosome Maturation In Uvrag-expressing Cellsmentioning

confidence: 99%

Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking

et al. 2008

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Autophagic and endocytic pathways are tightly regulated membrane rearrangement processes that are crucial for homeostasis, development and disease. Autophagic cargo is delivered from autophagosomes to lysosomes for degradation through a complex process that topologically resembles endosomal maturation. Here, we report that a Beclin1-binding autophagic tumour suppressor, UVRAG, interacts with the class C Vps complex, a key component of the endosomal fusion machinery. This interaction stimulates Rab7 GTPase activity and autophagosome fusion with late endosomes/lysosomes, thereby enhancing delivery and degradation of autophagic cargo. Furthermore, the UVRAG-class-C-Vps complex accelerates endosome-endosome fusion, resulting in rapid degradation of endocytic cargo. Remarkably, autophagosome/endosome maturation mediated by the UVRAG-class-C-Vps complex is genetically separable from UVRAG-Beclin1-mediated autophagosome formation. This result indicates that UVRAG functions as a multivalent trafficking effector that regulates not only two important steps of autophagy -autophagosome formation and maturation -but also endosomal fusion, which concomitantly promotes transport of autophagic and endocytic cargo to the degradative compartments.© 2008 Macmillan Publishers Limited. All rights reserved. 6 Correspondence should be addressed to J.U.J. (jaeujung@usc.edu). AUTHOR CONTRIBUTIONS C.L. performed all aspects of this study; L.S., K.I., M.G., Q.L. and P.F. assisted with the experimental design and in collecting the data; E.R., I.V. and V.D. assisted with the autophagic protein degradation and in vitro endosome fusion assay; C.A. provided Vps constructs and their antibodies; C.L. and J.J. organized this study and wrote the paper. All authors discussed the results and commented on the manuscript.Note: Supplementary Information is available on the Nature Cell Biology website. COMPETING FINANCIAL INTERESTSThe authors declare no competing financial interests.Reprints and permissions information is available online at http://npg.nature.com/reprintsandpermissions/ NIH Public Access Author ManuscriptNat Cell Biol. Author manuscript; available in PMC 2010 May 31. Published in final edited form as:Nat Cell Biol. 2008 July ; 10(7): 776-787. doi:10.1038/ncb1740. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptAutophagy is a tightly regulated membrane rearrangement process that ensures lysosomedependent bulk degradation of cytosolic proteins or organelles, and is highly conserved in eukaryotic cells, as seen with the endocytic pathway 1 . In response to environmental stresses, portions of cytoplasmic constituents are engulfed by a unique membrane structure, the phagophore, as it elongates to form a double-or multiple-membrane-bound compartment called the autophagosome. Newly synthesized autophagosomes then undergo extensive remodelling to acquire degradative capabilities. The remodelling process, also known as autophagosomal maturation, involves sequential fusion of autophagosomes with endocytic vesicles...

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“…In addition, diploids that were homozygous for pep8 lacked any sporulation defects. Because most of the other vacuolar biogenesis mutants isolated exhibit a defect in one of the above phenotypes, it appears from these studies on the pep8 disruptants that vacuolar biogenesis per se was not affected in these mutants (Banta et al 1990;Wada et al 1990;Woolford et al 1990;Preston et al 1991;Robinson et al 1991;Raymond et al 1992).…”

Section: Disruption Of the Pep8 Gene Leads To A Defect In The Processmentioning

confidence: 99%

“…This is in contrast to the other vacuolar biogenesis/sorting mutants. PEP3 is a gene required for vacuolar biogenesis/sorting, and cells bearing a disruption in PEP3 have been shown to secrete large amounts of the P2 precursor of CpY (Preston et al 1991;Robinson et al 1991). To determine whether the precursor form that remained intracellular was processed to mature form in pep3A-bearing cells and compare it with the intracellular processing of pep8/t cells, we carried out a kinetic analysis on the two mutants; the results are shown in Figure 5.…”

Section: Cpymentioning

confidence: 99%

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

Bachhawat¹,

Suhan²,

Jones³

1994

Genes Dev.

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A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation.

Cited by 77 publications

References 33 publications

A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.

A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.

Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking

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

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