ArticleCellular logistics2012
The SMS domain of Trs23p is responsible for the in vitro appearance of the TRAPP I complex in Saccharomyces cerevisiae.
Article in Cellular logistics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Stepwise Humanization of the Yeast TRAPP Core Enables Functional Analysis of TRAPP Variants.Cells · 2026Article
- Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.JACC. Basic to translational science · 2023Article
- The TRAPP complexes: discriminating GTPases in context.FEBS letters · 2023Review
- Cryo-EM structure of metazoan TRAPPIII, the multi-subunit complex that activates the GTPase Rab1.The EMBO journal · 2021Article
- The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020Review
- Deficiencies in vesicular transport mediated by TRAPPC4 are associated with severe syndromic intellectual disability.Brain : a journal of neurology · 2020Article
- Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein.Scientific reports · 2019Article
- Ypt/Rab GTPases and their TRAPP GEFs at the Golgi.FEBS letters · 2019Review
- The TRAPPIII complex activates the GTPase Ypt1 (Rab1) in the secretory pathway.The Journal of cell biology · 2018Article
- Article
- TRAPP Complexes in Secretion and Autophagy.Frontiers in cell and developmental biology · 2016Review
- Trs20 is required for TRAPP II assembly.Traffic (Copenhagen, Denmark) · 2013Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Saccharomyces cerevisiae transport protein particle (TRAPP) is a family of related multisubunit complexes required for endoplasmic reticulum-to-Golgi transport (TRAPP I), endosome-to-Golgi transport (TRAPP II) or cytosol to vacuole targeting (TRAPP III). To gain insight into the relationship between these complexes, we generated random and targeted mutations in the Trs23p core subunit. Remarkably, at physiological salt concentrations only two peaks (TRAPP I and a high molecular weight peak) are detected in wild-type cells. As the salt was raised, the high molecular weight peak resolved into TRAPP II and III peaks. Deletion of a Saccharomycotina-specific domain of Trs23p resulted in destabilization of TRAPP I but had no effect on TRAPP II or III. This mutation had no observable growth phenotype, normal levels of Ypt1p-directed guanine nucleotide exchange factor activity in vivo and did not display any in vivo nor in vitro blocks in membrane traffic. Biochemical analysis indicated that TRAPP I could be produced from the TRAPP II/III peak in vitro by increasing the salt concentration. Our data suggest that the SMS domain of Trs23p is responsible for the in vitro appearance of TRAPP I in S. cerevisiae. The implications of these findings are discussed.
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Registered trials
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.