ArticleMolecular biology of the cell2005
Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- HOPS-dependent vesicle tethering lock inhibits endolysosomal fusions and autophagosome secretion upon the loss of Syntaxin17.Science advances · 2025Article
- Heptad stereotypy, S/Q layering, and remote origin of the SARS-CoV-2 fusion core.Virus evolution · 2022Article
- An interaction network between the SNARE VAMP7 and Rab GTPases within a ciliary membrane-targeting complex.Journal of cell science · 2018Article
- Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.PLoS genetics · 2018Article
- Multiple ER-Golgi SNARE transmembrane domains are dispensable for trafficking but required for SNARE recycling.Molecular biology of the cell · 2016Article
- Granule cargo release from bone marrow-derived cells sustains cardiac hypertrophy.American journal of physiology. Heart and circulatory physiology · 2014Article
- Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing SNARE-specific chaperone NSF.Eukaryotic cell · 2010Article
- Binding interactions control SNARE specificity in vivo.The Journal of cell biology · 2008Article
- A SNARE complex unique to seed plants is required for protein storage vacuole biogenesis and seed development of Arabidopsis thaliana.The Plant cell · 2008Article
- Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes form bundles of four parallel alpha-helices. The central '0' layer of interacting amino acid side chains is highly conserved and contains one arginine and three glutamines, leading to the classification of SNAREs into R, Qa, Qb, and Qc-SNAREs. Replacing one of the glutamines with arginine in the yeast exocytotic SNARE complex is either lethal or causes a conditional growth defect that is compensated by replacing the R-SNARE arginine with glutamine. Using the yeast SNARE complex mediating traffic from the endoplasmic reticulum to the Golgi apparatus, we now show that functionally interacting SNAREs can be mapped by systematically exchanging glutamines and arginines in the '0' layer. The Q-->R replacement in the Qb-SNARE Bos1p has the strongest effect and can be alleviated by an Q-->R replacement in the R-SNARE Sec22p. Four Q residues in the central layer caused growth defects above 30 degrees C that were rescued by Q-->R substitutions in the Qa and Qc SNAREs Sed5p and Bet1p, respectively. The sec22(Q)/sed5(R) mutant is temperature sensitive and is rescued by a compensating R-->Q replacement in the R-SNARE Ykt6p. This rescue is attributed to the involvement of Sed5p and Ykt6p in a different SNARE complex that functions in intra-Golgi trafficking.
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