ArticleThe Journal of cell biology2000
Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
58 citing papers in PubMed, 145 citations in OpenAlex.
- Golgin Protein MoCoy1 Mediates Retrograde Trafficking From the Golgi to the ER, Regulating Fungal Development and Pathogenicity in Magnaporthe oryzae.Molecular plant pathology · 2025Article
- SNARE chaperone Sly1 directly mediates close-range vesicle tethering.The Journal of cell biology · 2024Article
- Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra-Golgi recycling vesicles.Traffic (Copenhagen, Denmark) · 2023Article
- Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson's Disease.International journal of molecular sciences · 2021Review
- Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport.Journal of cell science · 2020Article
- Multivalent Rab interactions determine tether-mediated membrane fusion.Molecular biology of the cell · 2017Article
- Sec24C/D-isoform-specific sorting of the preassembled ER-Golgi Q-SNARE complex.Molecular biology of the cell · 2016Article
- Overexpression of Sly41 suppresses COPII vesicle-tethering deficiencies by elevating intracellular calcium levels.Molecular biology of the cell · 2016Article
- Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins.Traffic (Copenhagen, Denmark) · 2016Article
- Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion.The Journal of biological chemistry · 2015Article
- Endomembrane trafficking protein SEC24A regulates cell size patterning in Arabidopsis.Plant physiology · 2014Article
- SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.eLife · 2014Article
- The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Review series: Rab GTPases and membrane identity: causal or inconsequential?The Journal of cell biology · 2013Review
- Retrograde traffic from the Golgi to the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Review
- The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi.Cold Spring Harbor perspectives in biology · 2013Review
- A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion.Bioarchitecture · 2012Article
- The yeast Rab GTPase Ypt1 modulates unfolded protein response dynamics by regulating the stability of HAC1 RNA.PLoS genetics · 2012Article
- Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Soluble NSF attachment protein receptor (SNARE) proteins are essential for membrane fusion in transport between the yeast ER and Golgi compartments. Subcellular fractionation experiments demonstrate that the ER/Golgi SNAREs Bos1p, Sec22p, Bet1p, Sed5p, and the Rab protein, Ypt1p, are distributed similarly but localize primarily with Golgi membranes. All of these SNARE proteins are efficiently packaged into COPII vesicles and suggest a dynamic cycling of SNARE machinery between ER and Golgi compartments. Ypt1p is not efficiently packaged into vesicles under these conditions. To determine in which membranes protein function is required, temperature-sensitive alleles of BOS1, BET1, SED5, SLY1, and YPT1 that prevent ER/Golgi transport in vitro at restrictive temperatures were used to selectively inactivate these gene products on vesicles or on Golgi membranes. Vesicles bearing mutations in Bet1p or Bos1p inhibit fusion with wild-type acceptor membranes, but acceptor membranes containing these mutations are fully functional. In contrast, vesicles bearing mutations in Sed5p, Sly1p, or Ypt1p are functional, whereas acceptor membranes containing these mutations block fusion. Thus, this set of SNARE proteins is symmetrically distributed between vesicle and acceptor compartments, but they function asymmetrically such that Bet1p and Bos1p are required on vesicles and Sed5p activity is required on acceptor membranes. We propose the asymmetry in SNARE protein function is maintained by an asymmetric distribution and requirement for the Ypt1p GTPase in this fusion event. When a transmembrane-anchored form of Ypt1p is used to restrict this GTPase to the acceptor compartment, vesicles depleted of Ypt1p remain competent for fusion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.