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Cholera Toxin as a Probe for Membrane Biology
Cholera toxin B-subunit (CTxB) has emerged as one of the most widely utilized tools in membrane biology and biophysics. CTxB is a homopentameric stable protein that binds tightly to up to five GM1 glycosphingolipids. This provides a robust and tractable model for exploring membrane structure and its...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402489/ https://www.ncbi.nlm.nih.gov/pubmed/34437414 http://dx.doi.org/10.3390/toxins13080543 |
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author | Kenworthy, Anne K. Schmieder, Stefanie S. Raghunathan, Krishnan Tiwari, Ajit Wang, Ting Kelly, Christopher V. Lencer, Wayne I. |
author_facet | Kenworthy, Anne K. Schmieder, Stefanie S. Raghunathan, Krishnan Tiwari, Ajit Wang, Ting Kelly, Christopher V. Lencer, Wayne I. |
author_sort | Kenworthy, Anne K. |
collection | PubMed |
description | Cholera toxin B-subunit (CTxB) has emerged as one of the most widely utilized tools in membrane biology and biophysics. CTxB is a homopentameric stable protein that binds tightly to up to five GM1 glycosphingolipids. This provides a robust and tractable model for exploring membrane structure and its dynamics including vesicular trafficking and nanodomain assembly. Here, we review important advances in these fields enabled by use of CTxB and its lipid receptor GM1. |
format | Online Article Text |
id | pubmed-8402489 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84024892021-08-29 Cholera Toxin as a Probe for Membrane Biology Kenworthy, Anne K. Schmieder, Stefanie S. Raghunathan, Krishnan Tiwari, Ajit Wang, Ting Kelly, Christopher V. Lencer, Wayne I. Toxins (Basel) Review Cholera toxin B-subunit (CTxB) has emerged as one of the most widely utilized tools in membrane biology and biophysics. CTxB is a homopentameric stable protein that binds tightly to up to five GM1 glycosphingolipids. This provides a robust and tractable model for exploring membrane structure and its dynamics including vesicular trafficking and nanodomain assembly. Here, we review important advances in these fields enabled by use of CTxB and its lipid receptor GM1. MDPI 2021-08-03 /pmc/articles/PMC8402489/ /pubmed/34437414 http://dx.doi.org/10.3390/toxins13080543 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Kenworthy, Anne K. Schmieder, Stefanie S. Raghunathan, Krishnan Tiwari, Ajit Wang, Ting Kelly, Christopher V. Lencer, Wayne I. Cholera Toxin as a Probe for Membrane Biology |
title | Cholera Toxin as a Probe for Membrane Biology |
title_full | Cholera Toxin as a Probe for Membrane Biology |
title_fullStr | Cholera Toxin as a Probe for Membrane Biology |
title_full_unstemmed | Cholera Toxin as a Probe for Membrane Biology |
title_short | Cholera Toxin as a Probe for Membrane Biology |
title_sort | cholera toxin as a probe for membrane biology |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402489/ https://www.ncbi.nlm.nih.gov/pubmed/34437414 http://dx.doi.org/10.3390/toxins13080543 |
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