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mDia1-3 in mammalian filopodia
mDia proteins are members of the formin family of actin nucleating proteins that polymerize linear actin filaments. Such filaments form the core of thin, tubular, membrane-bound cell surface protrusions known as filopodia, which are a major feature of mammalian cell morphology. Filopodia are dynamic...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3460838/ https://www.ncbi.nlm.nih.gov/pubmed/23060957 http://dx.doi.org/10.4161/cib.20214 |
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author | Goh, Wah Ing Ahmed, Sohail |
author_facet | Goh, Wah Ing Ahmed, Sohail |
author_sort | Goh, Wah Ing |
collection | PubMed |
description | mDia proteins are members of the formin family of actin nucleating proteins that polymerize linear actin filaments. Such filaments form the core of thin, tubular, membrane-bound cell surface protrusions known as filopodia, which are a major feature of mammalian cell morphology. Filopodia are dynamic structures that help cells sense environmental cues, and play a role in cell migration, axon guidance, angiogenesis and other processes. RhoGTPases bind to and control the activity of mDia proteins, and several other binding partners of the three mDia1 isoforms—mDia1, mDia2 and mDia3—have been documented. Two independent pathways controlling mammalian filopodium formation have emerged, with one driven by the RhoGTPase Cdc42, and the other by Rif. While mDia2 has been the main formin implicated in forming filopodia, mDia1 has recently surfaced as the key formin utilized by both the Cdc42 and Rif pathways to drive filopodial protrusion. |
format | Online Article Text |
id | pubmed-3460838 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-34608382012-10-11 mDia1-3 in mammalian filopodia Goh, Wah Ing Ahmed, Sohail Commun Integr Biol Mini Review mDia proteins are members of the formin family of actin nucleating proteins that polymerize linear actin filaments. Such filaments form the core of thin, tubular, membrane-bound cell surface protrusions known as filopodia, which are a major feature of mammalian cell morphology. Filopodia are dynamic structures that help cells sense environmental cues, and play a role in cell migration, axon guidance, angiogenesis and other processes. RhoGTPases bind to and control the activity of mDia proteins, and several other binding partners of the three mDia1 isoforms—mDia1, mDia2 and mDia3—have been documented. Two independent pathways controlling mammalian filopodium formation have emerged, with one driven by the RhoGTPase Cdc42, and the other by Rif. While mDia2 has been the main formin implicated in forming filopodia, mDia1 has recently surfaced as the key formin utilized by both the Cdc42 and Rif pathways to drive filopodial protrusion. Landes Bioscience 2012-07-01 /pmc/articles/PMC3460838/ /pubmed/23060957 http://dx.doi.org/10.4161/cib.20214 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Mini Review Goh, Wah Ing Ahmed, Sohail mDia1-3 in mammalian filopodia |
title | mDia1-3 in mammalian filopodia |
title_full | mDia1-3 in mammalian filopodia |
title_fullStr | mDia1-3 in mammalian filopodia |
title_full_unstemmed | mDia1-3 in mammalian filopodia |
title_short | mDia1-3 in mammalian filopodia |
title_sort | mdia1-3 in mammalian filopodia |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3460838/ https://www.ncbi.nlm.nih.gov/pubmed/23060957 http://dx.doi.org/10.4161/cib.20214 |
work_keys_str_mv | AT gohwahing mdia13inmammalianfilopodia AT ahmedsohail mdia13inmammalianfilopodia |