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Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes
Protein-mediated membrane remodeling is a ubiquitous and critical process for proper cellular function. Inverse Bin/Amphiphysin/Rvs (I-BAR) domains drive local membrane deformation as a precursor to large-scale membrane remodeling. We employ a multiscale approach to provide the molecular mechanism o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6697384/ https://www.ncbi.nlm.nih.gov/pubmed/31349990 http://dx.doi.org/10.1016/j.bpj.2019.06.025 |
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author | Jarin, Zack Tsai, Feng-Ching Davtyan, Aram Pak, Alexander J. Bassereau, Patricia Voth, Gregory A. |
author_facet | Jarin, Zack Tsai, Feng-Ching Davtyan, Aram Pak, Alexander J. Bassereau, Patricia Voth, Gregory A. |
author_sort | Jarin, Zack |
collection | PubMed |
description | Protein-mediated membrane remodeling is a ubiquitous and critical process for proper cellular function. Inverse Bin/Amphiphysin/Rvs (I-BAR) domains drive local membrane deformation as a precursor to large-scale membrane remodeling. We employ a multiscale approach to provide the molecular mechanism of unusual I-BAR domain-driven membrane remodeling at a low protein surface concentration with near-atomistic detail. We generate a bottom-up coarse-grained model that demonstrates similar membrane-bound I-BAR domain aggregation behavior as our recent Mesoscopic Membrane with Explicit Proteins model. Together, these models bridge several length scales and reveal an aggregation behavior of I-BAR domains. We find that at low surface coverage (i.e., low bound protein density), I-BAR domains form transient, tip-to-tip strings on periodic flat membrane sheets. Inside of lipid bilayer tubules, we find linear aggregates parallel to the axis of the tubule. Finally, we find that I-BAR domains form tip-to-tip aggregates around the edges of membrane domes. These results are supported by in vitro experiments showing low curvature bulges surrounded by I-BAR domains on giant unilamellar vesicles. Overall, our models reveal new I-BAR domain aggregation behavior in membrane tubules and on the surface of vesicles at low surface concentration that add insight into how I-BAR domain proteins may contribute to certain aspects of membrane remodeling in cells. |
format | Online Article Text |
id | pubmed-6697384 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Biophysical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-66973842020-08-06 Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes Jarin, Zack Tsai, Feng-Ching Davtyan, Aram Pak, Alexander J. Bassereau, Patricia Voth, Gregory A. Biophys J Articles Protein-mediated membrane remodeling is a ubiquitous and critical process for proper cellular function. Inverse Bin/Amphiphysin/Rvs (I-BAR) domains drive local membrane deformation as a precursor to large-scale membrane remodeling. We employ a multiscale approach to provide the molecular mechanism of unusual I-BAR domain-driven membrane remodeling at a low protein surface concentration with near-atomistic detail. We generate a bottom-up coarse-grained model that demonstrates similar membrane-bound I-BAR domain aggregation behavior as our recent Mesoscopic Membrane with Explicit Proteins model. Together, these models bridge several length scales and reveal an aggregation behavior of I-BAR domains. We find that at low surface coverage (i.e., low bound protein density), I-BAR domains form transient, tip-to-tip strings on periodic flat membrane sheets. Inside of lipid bilayer tubules, we find linear aggregates parallel to the axis of the tubule. Finally, we find that I-BAR domains form tip-to-tip aggregates around the edges of membrane domes. These results are supported by in vitro experiments showing low curvature bulges surrounded by I-BAR domains on giant unilamellar vesicles. Overall, our models reveal new I-BAR domain aggregation behavior in membrane tubules and on the surface of vesicles at low surface concentration that add insight into how I-BAR domain proteins may contribute to certain aspects of membrane remodeling in cells. The Biophysical Society 2019-08-06 2019-07-02 /pmc/articles/PMC6697384/ /pubmed/31349990 http://dx.doi.org/10.1016/j.bpj.2019.06.025 Text en © 2019 Biophysical Society. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Articles Jarin, Zack Tsai, Feng-Ching Davtyan, Aram Pak, Alexander J. Bassereau, Patricia Voth, Gregory A. Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title | Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title_full | Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title_fullStr | Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title_full_unstemmed | Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title_short | Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes |
title_sort | unusual organization of i-bar proteins on tubular and vesicular membranes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6697384/ https://www.ncbi.nlm.nih.gov/pubmed/31349990 http://dx.doi.org/10.1016/j.bpj.2019.06.025 |
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