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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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Detalles Bibliográficos
Autor principal: TAKENAWA, Tadaomi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2010
Materias:
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.
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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
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