A conformational change in the alpha-subunit of coatomer induced by ligand binding to gamma-COP revealed by single-pair FRET
- PMID: 18182008
- DOI: 10.1111/j.1600-0854.2007.00697.x
A conformational change in the alpha-subunit of coatomer induced by ligand binding to gamma-COP revealed by single-pair FRET
Abstract
Formation of transport vesicles involves polymerization of cytoplasmic coat proteins (COP). In COPI vesicle biogenesis, the heptameric complex coatomer is recruited to donor membranes by the interaction of multiple coatomer subunits with the budding machinery. Specific binding to the trunk domain of gamma-COP by the Golgi membrane protein p23 induces a conformational change that causes polymerization of the complex. Using single-pair fluorescence resonance energy transfer, we find that this conformational change takes place in individual coatomer complexes, independent of each other, and that the conformational rearrangement induced in gamma-COP is transmitted within the complex to its alpha-subunit. We suggest that capture of membrane protein machinery triggers cage formation in the COPI system.
Similar articles
-
Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP.Traffic. 2007 May;8(5):582-93. doi: 10.1111/j.1600-0854.2007.00554.x. Traffic. 2007. PMID: 17451557
-
Structure of the cytoplasmic domain of p23 in solution: implications for the formation of COPI vesicles.Biochem Biophys Res Commun. 2000 May 10;271(2):401-8. doi: 10.1006/bbrc.2000.2511. Biochem Biophys Res Commun. 2000. PMID: 10799309
-
Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins.Mol Cell Biol. 2006 Nov;26(21):8011-21. doi: 10.1128/MCB.01055-06. Epub 2006 Aug 28. Mol Cell Biol. 2006. PMID: 16940185 Free PMC article.
-
The COPI system: molecular mechanisms and function.FEBS Lett. 2009 Sep 3;583(17):2701-9. doi: 10.1016/j.febslet.2009.07.032. Epub 2009 Jul 22. FEBS Lett. 2009. PMID: 19631211 Review.
-
Cdc42 and Cellular Polarity: Emerging Roles at the Golgi.Trends Cell Biol. 2016 Apr;26(4):241-248. doi: 10.1016/j.tcb.2015.11.003. Epub 2015 Dec 17. Trends Cell Biol. 2016. PMID: 26704441 Free PMC article. Review.
Cited by
-
The Molecular Architecture of Native BBSome Obtained by an Integrated Structural Approach.Structure. 2019 Sep 3;27(9):1384-1394.e4. doi: 10.1016/j.str.2019.06.006. Epub 2019 Jul 11. Structure. 2019. PMID: 31303482 Free PMC article.
-
Solid-State NMR Investigations of the MHC II Transmembrane Domains: Topological Equilibria and Lipid Interactions.J Membr Biol. 2019 Oct;252(4-5):371-384. doi: 10.1007/s00232-019-00071-8. Epub 2019 Jun 11. J Membr Biol. 2019. PMID: 31187155
-
A Novel Glycoproteomics Workflow Reveals Dynamic O-GlcNAcylation of COPγ1 as a Candidate Regulator of Protein Trafficking.Front Endocrinol (Lausanne). 2018 Oct 15;9:606. doi: 10.3389/fendo.2018.00606. eCollection 2018. Front Endocrinol (Lausanne). 2018. PMID: 30459710 Free PMC article.
-
Structural characterization of coatomer in its cytosolic state.Protein Cell. 2016 Aug;7(8):586-600. doi: 10.1007/s13238-016-0296-z. Epub 2016 Jul 29. Protein Cell. 2016. PMID: 27472951 Free PMC article.
-
p24 family proteins: key players in the regulation of trafficking along the secretory pathway.Protoplasma. 2016 Jul;253(4):967-85. doi: 10.1007/s00709-015-0858-6. Epub 2015 Jul 30. Protoplasma. 2016. PMID: 26224213 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
