ArticleProceedings of the National Academy of Sciences of the United States of America2006
Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 48 citations in OpenAlex.
- Stepwise Humanization of the Yeast TRAPP Core Enables Functional Analysis of TRAPP Variants.Cells · 2026Article
- Visualization of ER-to-Golgi trafficking of procollagen X.Cell structure and function · 2024Article
- Protein S-palmitoylation enhances profibrotic signaling in response to cadmium.Toxicology and applied pharmacology · 2024Article
- Bacterial gasdermins reveal an ancient mechanism of cell death.Science (New York, N.Y.) · 2022Article
- Insights into auto-RSC chemical biology · 2021Review
- Structural basis of TRAPPIII-mediated Rab1 activation.The EMBO journal · 2021Article
- Lipid-induced S-palmitoylation as a Vital Regulator of Cell Signaling and Disease Development.International journal of biological sciences · 2021Review
- Article
- Protein Palmitoylation and Its Role in Bacterial and Viral Infections.Frontiers in immunology · 2017Review
- Progress toward Understanding Protein S-acylation: Prospective in Plants.Frontiers in plant science · 2017Review
- 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
- Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate.The Journal of biological chemistry · 2014Article
- Palmitoylation of virus proteins.Biology of the cell · 2012Review
- An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel.The Journal of biological chemistry · 2012Article
- Ion channel regulation by protein palmitoylation.The Journal of biological chemistry · 2011Review
- Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants.Molecular & cellular proteomics : MCP · 2011Article
- 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
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bet3 is a component of the transport protein particle complex involved in vesicular trafficking to and through the Golgi complex. X-ray structural analysis of human and mouse Bet3 revealed a hydrophobic tunnel inside the protein, which is occupied by a fatty acid linked to cysteine-68. We show here that Bet3 has strong self-palmitoylating activity. Incubation of purified Bet3 with [3H]palmitoyl-CoA (Pal-CoA) leads to a rapid and stoichiometric attachment of fatty acids to cysteine-68. Bet3 has an intrinsic affinity for Pal-CoA, and the palmitoylation reaction occurs at physiological pH values and Pal-CoA concentrations. Moreover, Bet3 is also efficiently palmitoylated at cysteine-68 inside vertebrate cells. Palmitoylation can occur late after Bet3 synthesis, but once the fatty acids are bound they are not removed, not even by disassembly of the Golgi complex. Narrowing the hydrophobic tunnel by exchange of alanine-82 with bulkier amino acids inhibits palmitoylation, both in vitro and inside cells, indicating that the fatty acid must insert into the tunnel for stable attachment. Finally, we show that palmitoylation of Bet3 plays a structural role. CD spectroscopy reveals that chemically deacylated Bet3 has a reduced melting temperature. As a consequence of its structural defect nonacylated Bet3 does not bind to TPC6, a further subunit of the transport protein particle complex, and is degraded inside cells.
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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.