An N-End Rule Destabilization Mutant Reveals Pre-Golgi Requirements for Sec7p in Yeast Membrane Traffic

Wolf, Joseph R.; Nicks, Michael; Deitz, Stephen B.; Tuinen, E van; Franzusoff, Alex

doi:10.1006/bbrc.1998.8084

Cited by 19 publications

(20 citation statements)

References 35 publications

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“…The membrane-bound vacuolar ALP also displayed a normal electrophoretic pattern ( Figure 1A). Conversely, the precursor form of ALP (proALP) was detected in the sec7-1 mutant, which is defective in ER to Golgi and intra-Golgi transport (Franzusoff and Schekman, 1989;Wolf et al, 1998), and in the apm3⌬ mutant, which lacks one of the four subunits of the heterotetrameric adaptor protein complex AP-3 and is thus defective in the transport of ALP from the TGN to the vacuole (Cowles et al, 1997).…”

Section: The Vps55⌬ Strain Is Impaired In Trafficking From the Golgi mentioning

confidence: 99%

Yeast Vps55p, a Functional Homolog of Human Obesity Receptor Gene-related Protein, Is Involved in Late Endosome to Vacuole Trafficking

Belgareh‐Touzé

Avaro

Rouillé

et al. 2002

MBoC

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The Saccharomyces cerevisiae VPS55 (YJR044c) gene encodes a small protein of 140 amino acids with four potential transmembrane domains. VPS55 belongs to a family of genes of unknown function, including the human gene encoding the obesity receptor gene-related protein (OB-RGRP). Yeast cells with a disrupted VPS55 present normal vacuolar morphology, but exhibit an abnormal secretion of the Golgi form of the soluble vacuolar carboxypeptidase Y. However, trafficking of the membrane-bound vacuolar alkaline phosphatase remains normal. The endocytosis of uracil permease, used as an endocytic marker, is normal in vps55Delta cells, but its degradation is delayed and this marker transiently accumulates in late endosomal compartments. We also found that Vps55p is mainly localized in the late endosomes. Collectively, these results indicate that Vps55p is involved in late endosome to vacuole trafficking. Finally, we show that human OB-RGRP displays the same distribution as Vps55p and corrects the phenotypic defects of the vps55Delta strain. Therefore, the function of Vps55p has been conserved throughout evolution. This study highlights the importance of the multispanning Vps55p and OB-RGRP in membrane trafficking to the vacuole/lysosome of eukaryotic cells.

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Section: The Vps55⌬ Strain Is Impaired In Trafficking From the Golgi mentioning

confidence: 99%

Yeast Vps55p, a Functional Homolog of Human Obesity Receptor Gene-related Protein, Is Involved in Late Endosome to Vacuole Trafficking

Belgareh‐Touzé

Avaro

Rouillé

et al. 2002

MBoC

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“…Sec7p, Gea1p, and Gea2p are known to have roles in secretion (Peyroche et al, 1996;Wolf et al, 1998). Sec7p localizes to the trans-Golgi apparatus and is involved in COPI-mediated intraGolgi transport (Deitz et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Syt1p promotes activation of Arl1p at the late Golgi to recruit Imh1p

Chen

Tsai

Hsu

et al. 2010

Journal of Cell Science

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In yeast, Arl3p recruits Arl1p GTPase to regulate Golgi function and structure. However, the molecular mechanism involved in regulating activation of Arl1p at the Golgi is unknown. Here, we show that Syt1p promoted activation of Arl1p and recruitment of a golgin protein, Imh1p, to the Golgi. Deletion of SYT1 resulted in the majority of Arl1p being distributed diffusely throughout the cytosol. Overexpression of Syt1p increased Arl1p-GTP production in vivo and the Syt1-Sec7 domain promoted nucleotide exchange on Arl1p in vitro. Syt1p function required the N-terminal region, Sec7 and PH domains. Arl1p, but not Arl3p, interacted with Syt1p. Localization of Syt1p to the Golgi did not require Arl3p. Unlike arl1Δ or arl3Δ mutants, syt1Δ did not show defects in Gas1p transport, cell wall integrity or vacuolar structure. These findings reveal that activation of Arl1p is regulated in part by Syt1p, and imply that Arl1p activation, by using more than one GEF, exerts distinct biological activities at the Golgi compartment.

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“…The founding members, Sec7p of Saccharomyces cerevisiae and EMB30p of Arabidopsis thaliana, play an essential role at the cellular and developmental levels, respectively (1,17). In particular, Sec7p is required for the maintenance of functional Golgi cisternae and for vesicular transport between the endoplasmic reticulum and the Golgi complex (7,8,19). Other members, such as Gea1p/Gea2p and ARNO, have been also implicated in protein traffic (2,15) and seem to participate in the regulation of membrane homeostasis as a result of their genetic and biochemical interactions with ADP ribosylation factors (ARFs), known for mediating the recruitment of cytosolic coat proteins onto emerging vesicles and tubules (5,18).…”

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confidence: 99%

HumanGBF1Is a Ubiquitously Expressed Gene of the Sec7 Domain Family Mapping to 10q24

et al. 1998

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An N-End Rule Destabilization Mutant Reveals Pre-Golgi Requirements for Sec7p in Yeast Membrane Traffic

Cited by 19 publications

References 35 publications

Yeast Vps55p, a Functional Homolog of Human Obesity Receptor Gene-related Protein, Is Involved in Late Endosome to Vacuole Trafficking

Yeast Vps55p, a Functional Homolog of Human Obesity Receptor Gene-related Protein, Is Involved in Late Endosome to Vacuole Trafficking

Syt1p promotes activation of Arl1p at the late Golgi to recruit Imh1p

HumanGBF1Is a Ubiquitously Expressed Gene of the Sec7 Domain Family Mapping to 10q24

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