ArticleThe Journal of cell biology1997
Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
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Who cites it
120 citing papers in PubMed.
- Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026Review
- Cisternal Maturation of the Golgi Apparatus in Budding Yeast.Sub-cellular biochemistry · 2026Review
- Insights on the intracellular trafficking of calcifying medium in a reef-building coral.Communications biology · 2025Article
- Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024Review
- Spatiotemporal dissection of the Golgi apparatus and the ER-Golgi intermediate compartment in budding yeast.eLife · 2024Article
- Osh-dependent and -independent Regulation of PI4P Levels During Polarized Growth ofMolecular biology of the cell · 2023Article
- The yeast endocytic early/sorting compartment exists as an independent sub-compartment within theeLife · 2023Article
- The TRAPP complexes: discriminating GTPases in context.FEBS letters · 2023Review
- Actomyosin activity-dependent apical targeting of Rab11 vesicles reinforces apical constriction.The Journal of cell biology · 2022Article
- Structure of a TRAPPII-Rab11 activation intermediate reveals GTPase substrate selection mechanisms.Science advances · 2022Article
- The Golgi Apparatus and its Next-Door Neighbors.Frontiers in cell and developmental biology · 2022Review
- RAB14 GTPase is essential for actin-based asymmetric division during mouse oocyte maturation.Cell proliferation · 2021Article
- Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021Article
- Establishing Regulation of a Dynamic Process by Ypt/Rab GTPases : A Case for Cisternal Progression.Methods in molecular biology (Clifton, N.J.) · 2021Article
- To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021Review
- Protein markers forJournal of extracellular vesicles · 2020Article
- Off the wall: The rhyme and reason ofCell surface (Amsterdam, Netherlands) · 2019Review
- Ypt/Rab GTPases and their TRAPP GEFs at the Golgi.FEBS letters · 2019Review
- New approaches for solving old problems in neuronal protein trafficking.Molecular and cellular neurosciences · 2018Review
- Toolbox: Creating a systematic database of secretory pathway proteins uncovers new cargo for COPI.Traffic (Copenhagen, Denmark) · 2018Article
60 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Small GTPases of the Ypt/rab family are involved in the regulation of vesicular transport. These GTPases apparently function during the targeting of vesicles to the acceptor compartment. Two members of the Ypt/rab family, Ypt1p and Sec4p, have been shown to regulate early and late steps of the yeast exocytic pathway, respectively. Here we tested the role of two newly identified GTPases, Ypt31p and Ypt32p. These two proteins share 81% identity and 90% similarity, and belong to the same protein subfamily as Ypt1p and Sec4p. Yeast cells can tolerate deletion of either the YPT31 or the YPT32 gene, but not both. These observations suggest that Ypt31p and Ypt32p perform identical or overlapping functions. Cells deleted for the YPT31 gene and carrying a conditional ypt32 mutation exhibit protein transport defects in the late exocytic pathway, but not in vacuolar protein sorting. The ypt31/ 32 mutant secretory defect is clearly downstream from that displayed by a ypt1 mutant and is similar to that of sec4 mutant cells. However, electron microscopy revealed that while sec4 mutant cells accumulate secretory vesicles, ypt31/32 mutant cells accumulate aberrant Golgi structures. The ypt31/32 phenotype is epistatic to that of a sec1 mutant, which accumulates secretory vesicles. Together, these results indicate that the Ypt31/32p GTPases are required for a step that occurs in the trans-Golgi compartment, between the reactions regulated by Ypt1p and Sec4p. This step might involve budding of vesicles from the trans-Golgi. Alternatively, Ypt31/32p might promote secretion indirectly, by allowing fusion of recycling vesicles with the trans-Golgi compartment.
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