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Phosphoinositide-binding interface proteins involved in shaping cell membranes
The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, wh...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Japan Academy
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3108299/ https://www.ncbi.nlm.nih.gov/pubmed/20467216 http://dx.doi.org/10.2183/pjab.86.509 |
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author | TAKENAWA, Tadaomi |
author_facet | TAKENAWA, Tadaomi |
author_sort | TAKENAWA, Tadaomi |
collection | PubMed |
description | The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes. |
format | Online Article Text |
id | pubmed-3108299 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The Japan Academy |
record_format | MEDLINE/PubMed |
spelling | pubmed-31082992011-06-28 Phosphoinositide-binding interface proteins involved in shaping cell membranes TAKENAWA, Tadaomi Proc Jpn Acad Ser B Phys Biol Sci Review The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes. The Japan Academy 2010-05-11 /pmc/articles/PMC3108299/ /pubmed/20467216 http://dx.doi.org/10.2183/pjab.86.509 Text en © 2010 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review TAKENAWA, Tadaomi Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title | Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title_full | Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title_fullStr | Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title_full_unstemmed | Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title_short | Phosphoinositide-binding interface proteins involved in shaping cell membranes |
title_sort | phosphoinositide-binding interface proteins involved in shaping cell membranes |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3108299/ https://www.ncbi.nlm.nih.gov/pubmed/20467216 http://dx.doi.org/10.2183/pjab.86.509 |
work_keys_str_mv | AT takenawatadaomi phosphoinositidebindinginterfaceproteinsinvolvedinshapingcellmembranes |