Nonclassical Protein Sorting to the Yeast Vacuole

Klionsky, Daniel J.

doi:10.1074/jbc.273.18.10807

Cited by 61 publications

(61 citation statements)

References 52 publications

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“…API oligomerizes in the cytosol and is enclosed in a double membrane to form cytosol to vacuole transport (CVT) vesicles. A number of genes (CVT) have been identified that are required for API transport, and some CVT genes are identical to genes involved in autophagy or to genes required for vacuolar fusion in the CPY and ALP pathways (Klionsky, 1998). It is unclear whether traffic of API, CPY, and ALP converge at a common compartment before transport to the vacuole or whether membranes from these pathways fuse directly with vacuolar membranes.…”

Section: Introductionmentioning

confidence: 99%

“…In the CVT pathway a double membrane engulfs oligomerized cytosolic API to form CVT vesicles (Klionsky, 1997(Klionsky, , 1998. Because Vti1p is required for their vacuolar delivery, we assume that Vti1p is localized on the CVT vesicles.…”

Section: Implication For Vacuolar Membrane Trafficmentioning

confidence: 99%

“…Interacts with Vam3p in Traffic of API to the Vacuole API reaches the vacuole from the cytoplasm independently of the secretory pathway (Klionsky, 1997(Klionsky, , 1998. API is synthesized in the cytoplasm and packaged into vesicles with a double membrane, which fuse with the vacuole in a Vam3p-dependent reaction (Darsow et al, 1997).…”

Section: Vti1pmentioning

confidence: 99%

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TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

Mollard

Stevens

1999

MBoC

162

133

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The interaction between v-SNAREs on transport vesicles and t-SNAREs on target membranes is required for membrane traffic in eukaryotic cells. Here we identify Vti1p as the first v-SNARE protein found to be required for biosynthetic traffic into the yeast vacuole, the equivalent of the mammalian lysosome. Certain vti1-tsyeast mutants are defective in alkaline phosphatase transport from the Golgi to the vacuole and in targeting of aminopeptidase I from the cytosol to the vacuole. VTI1 interacts genetically with the vacuolar t-SNARE VAM3, which is required for transport of both alkaline phosphatase and aminopeptidase I to the vacuole. The v-SNARE Nyv1p forms a SNARE complex with Vam3p in homotypic vacuolar fusion; however, we find that Nyv1p is not required for any of the three biosynthetic pathways to the vacuole. v-SNAREs were thought to ensure specificity in membrane traffic. However, Vti1p also functions in two additional membrane traffic pathways: Vti1p interacts with the t-SNAREs Pep12p in traffic from the TGN to the prevacuolar compartment and with Sed5p in retrograde traffic to the cis-Golgi. The ability of Vti1p to mediate multiple fusion steps requires additional proteins to ensure specificity in membrane traffic.

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Section: Introductionmentioning

confidence: 99%

Section: Implication For Vacuolar Membrane Trafficmentioning

confidence: 99%

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TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

Mollard

Stevens

1999

MBoC

162

133

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“…These studies therefore indicate that the Ras/PKA pathway must be inhibiting an early step in the autophagy pathway, a step that precedes (or is required for) the formation of the autophagosome. (21,76). Cvt transport occurs constitutively in growing cells and represents an alternative delivery route to the traditional secretory pathway (21,58).…”

Section: Elevated Levels Of Ras/pka Signaling Activity Inhibited the mentioning

confidence: 99%

“…The hydrolytic enzymes within the vacuole then degrade both the delimiting membrane and the contents of the autophagic body (19 -22). When this pathway is fully induced, it is generally responsible for the majority of the protein and membrane turnover occurring in those cells (21,23).…”

mentioning

confidence: 99%

The Ras/cAMP-dependent Protein Kinase Signaling Pathway Regulates an Early Step of the Autophagy Process in Saccharomyces cerevisiae

Budovskaya

Stephan

Reggiori

et al. 2004

Journal of Biological Chemistry

Self Cite

194

168

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When faced with nutrient deprivation, Saccharomyces cerevisiae cells enter into a nondividing resting state, known as stationary phase. The Ras/PKA (cAMPdependent protein kinase) signaling pathway plays an important role in regulating the entry into this resting state and the subsequent survival of stationary phase cells. The survival of these resting cells is also dependent upon autophagy, a membrane trafficking pathway that is induced upon nutrient deprivation. Autophagy is responsible for targeting bulk protein and other cytoplasmic constituents to the vacuolar compartment for their ultimate degradation. The data presented here demonstrate that the Ras/PKA signaling pathway inhibits an early step in autophagy because mutants with elevated levels of Ras/PKA activity fail to accumulate transport intermediates normally associated with this process. Quantitative assays indicate that these increased levels of Ras/PKA signaling activity result in an essentially complete block to autophagy. Interestingly, Ras/PKA activity also inhibited a related process, the cytoplasm to vacuole targeting (Cvt) pathway that is responsible for the delivery of a subset of vacuolar proteins in growing cells. These data therefore indicate that the Ras/PKA signaling pathway is not regulating a switch between the autophagy and Cvt modes of transport. Instead, it is more likely that this signaling pathway is controlling an activity that is required during the early stages of both of these membrane trafficking pathways. Finally, the data suggest that at least a portion of the Ras/PKA effects on stationary phase survival are the result of the regulation of autophagy activity by this signaling pathway.

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Aminopeptidase yscCo-II: a new cobalt-dependent aminopeptidase from yeast?purification and biochemical characterization

Herrera‐Camacho

Morales‐Monterrosas

Quiróz‐Alvarez³

2000

Yeast

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Nonclassical Protein Sorting to the Yeast Vacuole

Cited by 61 publications

References 52 publications

TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

The Ras/cAMP-dependent Protein Kinase Signaling Pathway Regulates an Early Step of the Autophagy Process in Saccharomyces cerevisiae

Aminopeptidase yscCo-II: a new cobalt-dependent aminopeptidase from yeast?purification and biochemical characterization

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