ArticleThe EMBO journal2005
Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 57 citations in OpenAlex.
- Stepwise Humanization of the Yeast TRAPP Core Enables Functional Analysis of TRAPP Variants.Cells · 2026Article
- Autopalmitoylation of IDH1-R132H regulates its neomorphic activity in cancer cells.Nature chemical biology · 2026Article
- The palmitoylation of gasdermin D directs its membrane translocation and pore formation during pyroptosis.Science immunology · 2024Article
- The TRAPP complexes: discriminating GTPases in context.FEBS letters · 2023Review
- The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.FEBS letters · 2023Review
- Insights into auto-RSC chemical biology · 2021Review
- Structural basis of TRAPPIII-mediated Rab1 activation.The EMBO journal · 2021Article
- Structure and Mechanism of DHHC Protein Acyltransferases.Journal of molecular biology · 2020Review
- Protein Lipidation in Cell Signaling and Diseases: Function, Regulation, and Therapeutic Opportunities.Cell chemical biology · 2018Review
- Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.Scientific reports · 2017Article
- Membrane skeletal association and post-translational allosteric regulation of Toxoplasma gondii GAPDH1.Molecular microbiology · 2017Article
- Fatty acylation of proteins: The long and the short of it.Progress in lipid research · 2016Review
- Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway.Nature chemical biology · 2016Article
- The predominant species of nonstructural protein 4B in hepatitis C virus-replicating cells is not palmitoylated.The Journal of general virology · 2015Article
- Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex.The Journal of biological chemistry · 2012Article
- Mutational analysis of the yeast TRAPP subunit Trs20p identifies roles in endocytic recycling and sporulation.PloS one · 2012Article
- Structure and mechanism in membrane trafficking.Current opinion in cell biology · 2010Review
- Characterization of the self-palmitoylation activity of the transport protein particle component Bet3.Cellular and molecular life sciences : CMLS · 2010Article
- The TRAPP complex: insights into its architecture and function.Traffic (Copenhagen, Denmark) · 2008Review
- The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.Cell · 2008Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BET3 is a component of TRAPP, a complex involved in the tethering of transport vesicles to the cis-Golgi membrane. The crystal structure of human BET3 has been determined to 1.55-A resolution. BET3 adopts an alpha/beta-plait fold and forms dimers in the crystal and in solution, which predetermines the architecture of TRAPP where subunits are present in equimolar stoichiometry. A hydrophobic pocket within BET3 buries a palmitate bound through a thioester linkage to cysteine 68. BET3 and yeast Bet3p are palmitoylated in recombinant yeast cells, the mutant proteins BET3 C68S and Bet3p C80S remain unmodified. Both BET3 and BET3 C68S are found in membrane and cytosolic fractions of these cells; in membrane extractions, they behave like tightly membrane-associated proteins. In a deletion strain, both Bet3p and Bet3p C80S rescue cell viability. Thus, palmitoylation is neither required for viability nor sufficient for membrane association of BET3, which may depend on protein-protein contacts within TRAPP or additional, yet unidentified modifications of BET3. A conformational change may facilitate palmitoyl extrusion from BET3 and allow the fatty acid chain to engage in intermolecular hydrophobic interactions.
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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.