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Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2

BACKGROUND: The Scar/WAVE family of proteins mediates signals to actin assembly by direct activation of the Arp2/3 complex. These proteins have been characterised as major regulators of lamellipodia formation downstream of Rac activation and as members of large protein complexes. RESULTS: We have in...

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Detalles Bibliográficos
Autores principales: Stovold, Craig F, Millard, Thomas H, Machesky, Laura M
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC555569/
https://www.ncbi.nlm.nih.gov/pubmed/15752430
http://dx.doi.org/10.1186/1471-2121-6-11
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author Stovold, Craig F
Millard, Thomas H
Machesky, Laura M
author_facet Stovold, Craig F
Millard, Thomas H
Machesky, Laura M
author_sort Stovold, Craig F
collection PubMed
description BACKGROUND: The Scar/WAVE family of proteins mediates signals to actin assembly by direct activation of the Arp2/3 complex. These proteins have been characterised as major regulators of lamellipodia formation downstream of Rac activation and as members of large protein complexes. RESULTS: We have investigated the interactions of the three human Scar/WAVE isoforms with several previously described binding partners for Scar/WAVE 1 or 2. We find that all three Scar/WAVE isoforms behave similarly and are likely to participate in the same kinds of protein complexes that regulate actin assembly. CONCLUSION: Differences between Scar/WAVE proteins are therefore likely to be at the level of tissue distribution or subtle differences in the affinity for specific binding partners.
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spelling pubmed-5555692005-03-25 Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2 Stovold, Craig F Millard, Thomas H Machesky, Laura M BMC Cell Biol Research Article BACKGROUND: The Scar/WAVE family of proteins mediates signals to actin assembly by direct activation of the Arp2/3 complex. These proteins have been characterised as major regulators of lamellipodia formation downstream of Rac activation and as members of large protein complexes. RESULTS: We have investigated the interactions of the three human Scar/WAVE isoforms with several previously described binding partners for Scar/WAVE 1 or 2. We find that all three Scar/WAVE isoforms behave similarly and are likely to participate in the same kinds of protein complexes that regulate actin assembly. CONCLUSION: Differences between Scar/WAVE proteins are therefore likely to be at the level of tissue distribution or subtle differences in the affinity for specific binding partners. BioMed Central 2005-03-07 /pmc/articles/PMC555569/ /pubmed/15752430 http://dx.doi.org/10.1186/1471-2121-6-11 Text en Copyright © 2005 Stovold et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Stovold, Craig F
Millard, Thomas H
Machesky, Laura M
Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title_full Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title_fullStr Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title_full_unstemmed Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title_short Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
title_sort inclusion of scar/wave3 in a similar complex to scar/wave1 and 2
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC555569/
https://www.ncbi.nlm.nih.gov/pubmed/15752430
http://dx.doi.org/10.1186/1471-2121-6-11
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