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Attachment of Rod-Like (BAR) Proteins and Membrane Shape
Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a majo...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Bentham Science Publishers Ltd
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343385/ https://www.ncbi.nlm.nih.gov/pubmed/21428902 http://dx.doi.org/10.2174/138955711795305353 |
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author | Kabaso, D Gongadze, E Elter, P van Rienen, U Gimsa, J Kralj-Iglič, V Iglič, A |
author_facet | Kabaso, D Gongadze, E Elter, P van Rienen, U Gimsa, J Kralj-Iglič, V Iglič, A |
author_sort | Kabaso, D |
collection | PubMed |
description | Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a major role in various biological processes such as cell motility and cell growth. Different models of binding of BAR domains to the lipid bilayer are described. The binding includes hydrophobic insertion loops and electrostatic interactions between basic amino acids at the concave region of the BAR domain and negatively charged lipids. To shed light on the elusive binding dynamics, a novel experiment is proposed to expand the technique of single-molecule AFM for the traction of binding energy of a single BAR domain. |
format | Online Article Text |
id | pubmed-3343385 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Bentham Science Publishers Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-33433852012-05-04 Attachment of Rod-Like (BAR) Proteins and Membrane Shape Kabaso, D Gongadze, E Elter, P van Rienen, U Gimsa, J Kralj-Iglič, V Iglič, A Mini Rev Med Chem Article Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a major role in various biological processes such as cell motility and cell growth. Different models of binding of BAR domains to the lipid bilayer are described. The binding includes hydrophobic insertion loops and electrostatic interactions between basic amino acids at the concave region of the BAR domain and negatively charged lipids. To shed light on the elusive binding dynamics, a novel experiment is proposed to expand the technique of single-molecule AFM for the traction of binding energy of a single BAR domain. Bentham Science Publishers Ltd 2011-04 2011-04 /pmc/articles/PMC3343385/ /pubmed/21428902 http://dx.doi.org/10.2174/138955711795305353 Text en © 2011 Bentham Science Publishers Ltd. http://creativecommons.org/licenses/by/2.5/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Article Kabaso, D Gongadze, E Elter, P van Rienen, U Gimsa, J Kralj-Iglič, V Iglič, A Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title | Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title_full | Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title_fullStr | Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title_full_unstemmed | Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title_short | Attachment of Rod-Like (BAR) Proteins and Membrane Shape |
title_sort | attachment of rod-like (bar) proteins and membrane shape |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343385/ https://www.ncbi.nlm.nih.gov/pubmed/21428902 http://dx.doi.org/10.2174/138955711795305353 |
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