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Modest Effects of Lipid Modifications on the Structure of Caveolin-3
[Image: see text] Caveolin-3 (Cav3) is an unconventional membrane protein that serves as a critical scaffolding hub in caveolae and is genetically linked to various muscle disorders. In this work, we report the expression, purification, and characterization of full-length human Cav3. To mimic the pa...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100780/ https://www.ncbi.nlm.nih.gov/pubmed/24960539 http://dx.doi.org/10.1021/bi5005238 |
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author | Kim, Ji-Hun Peng, Dungeng Schlebach, Jonathan P. Hadziselimovic, Arina Sanders, Charles R. |
author_facet | Kim, Ji-Hun Peng, Dungeng Schlebach, Jonathan P. Hadziselimovic, Arina Sanders, Charles R. |
author_sort | Kim, Ji-Hun |
collection | PubMed |
description | [Image: see text] Caveolin-3 (Cav3) is an unconventional membrane protein that serves as a critical scaffolding hub in caveolae and is genetically linked to various muscle disorders. In this work, we report the expression, purification, and characterization of full-length human Cav3. To mimic the palmitoylation of endogenous Cav3, we developed a generally applicable approach to covalently attached thioalkyl chains at natively modified cysteine residues. Nuclear magnetic resonance measurements indicate that lipidation exerts only a modest and local effect on the Cav3 structure, with little impact on the structures of the N-terminal domain, the scaffolding domain, and the extreme C-terminus. |
format | Online Article Text |
id | pubmed-4100780 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-41007802015-06-24 Modest Effects of Lipid Modifications on the Structure of Caveolin-3 Kim, Ji-Hun Peng, Dungeng Schlebach, Jonathan P. Hadziselimovic, Arina Sanders, Charles R. Biochemistry [Image: see text] Caveolin-3 (Cav3) is an unconventional membrane protein that serves as a critical scaffolding hub in caveolae and is genetically linked to various muscle disorders. In this work, we report the expression, purification, and characterization of full-length human Cav3. To mimic the palmitoylation of endogenous Cav3, we developed a generally applicable approach to covalently attached thioalkyl chains at natively modified cysteine residues. Nuclear magnetic resonance measurements indicate that lipidation exerts only a modest and local effect on the Cav3 structure, with little impact on the structures of the N-terminal domain, the scaffolding domain, and the extreme C-terminus. American Chemical Society 2014-06-24 2014-07-15 /pmc/articles/PMC4100780/ /pubmed/24960539 http://dx.doi.org/10.1021/bi5005238 Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) |
spellingShingle | Kim, Ji-Hun Peng, Dungeng Schlebach, Jonathan P. Hadziselimovic, Arina Sanders, Charles R. Modest Effects of Lipid Modifications on the Structure of Caveolin-3 |
title | Modest Effects of Lipid Modifications on the Structure
of Caveolin-3 |
title_full | Modest Effects of Lipid Modifications on the Structure
of Caveolin-3 |
title_fullStr | Modest Effects of Lipid Modifications on the Structure
of Caveolin-3 |
title_full_unstemmed | Modest Effects of Lipid Modifications on the Structure
of Caveolin-3 |
title_short | Modest Effects of Lipid Modifications on the Structure
of Caveolin-3 |
title_sort | modest effects of lipid modifications on the structure
of caveolin-3 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100780/ https://www.ncbi.nlm.nih.gov/pubmed/24960539 http://dx.doi.org/10.1021/bi5005238 |
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