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The WASP and WAVE family proteins
All eukaryotic cells need to reorganize their actin cytoskeleton to change shape, divide, move, and take up nutrients for survival. The Wiskott-Aldrich syndrome protein (WASP) and WASP-family verprolin-homologous protein (WAVE) family proteins are fundamental actin-cytoskeleton reorganizers found th...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718491/ https://www.ncbi.nlm.nih.gov/pubmed/19589182 http://dx.doi.org/10.1186/gb-2009-10-6-226 |
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author | Kurisu, Shusaku Takenawa, Tadaomi |
author_facet | Kurisu, Shusaku Takenawa, Tadaomi |
author_sort | Kurisu, Shusaku |
collection | PubMed |
description | All eukaryotic cells need to reorganize their actin cytoskeleton to change shape, divide, move, and take up nutrients for survival. The Wiskott-Aldrich syndrome protein (WASP) and WASP-family verprolin-homologous protein (WAVE) family proteins are fundamental actin-cytoskeleton reorganizers found throughout the eukaryotes. The conserved function across species is to receive upstream signals from Rho-family small GTPases and send them to activate the Arp2/3 complex, leading to rapid actin polymerization, which is critical for cellular processes such as endocytosis and cell motility. Molecular and cell biological studies have identified a wide array of regulatory molecules that bind to the WASP and WAVE proteins and give them diversified roles in distinct cellular locations. Genetic studies using model organisms have also improved our understanding of how the WASP- and WAVE-family proteins act to shape complex tissue architectures. Current efforts are focusing on integrating these pieces of molecular information to draw a unified picture of how the actin cytoskeleton in a single cell works dynamically to build multicellular organization. |
format | Text |
id | pubmed-2718491 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-27184912010-06-15 The WASP and WAVE family proteins Kurisu, Shusaku Takenawa, Tadaomi Genome Biol Protein Family Review All eukaryotic cells need to reorganize their actin cytoskeleton to change shape, divide, move, and take up nutrients for survival. The Wiskott-Aldrich syndrome protein (WASP) and WASP-family verprolin-homologous protein (WAVE) family proteins are fundamental actin-cytoskeleton reorganizers found throughout the eukaryotes. The conserved function across species is to receive upstream signals from Rho-family small GTPases and send them to activate the Arp2/3 complex, leading to rapid actin polymerization, which is critical for cellular processes such as endocytosis and cell motility. Molecular and cell biological studies have identified a wide array of regulatory molecules that bind to the WASP and WAVE proteins and give them diversified roles in distinct cellular locations. Genetic studies using model organisms have also improved our understanding of how the WASP- and WAVE-family proteins act to shape complex tissue architectures. Current efforts are focusing on integrating these pieces of molecular information to draw a unified picture of how the actin cytoskeleton in a single cell works dynamically to build multicellular organization. BioMed Central 2009 2009-06-15 /pmc/articles/PMC2718491/ /pubmed/19589182 http://dx.doi.org/10.1186/gb-2009-10-6-226 Text en Copyright © 2009 BioMed Central Ltd |
spellingShingle | Protein Family Review Kurisu, Shusaku Takenawa, Tadaomi The WASP and WAVE family proteins |
title | The WASP and WAVE family proteins |
title_full | The WASP and WAVE family proteins |
title_fullStr | The WASP and WAVE family proteins |
title_full_unstemmed | The WASP and WAVE family proteins |
title_short | The WASP and WAVE family proteins |
title_sort | wasp and wave family proteins |
topic | Protein Family Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718491/ https://www.ncbi.nlm.nih.gov/pubmed/19589182 http://dx.doi.org/10.1186/gb-2009-10-6-226 |
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