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

Craig F. Stovold; Thomas H. Millard; Laura M. Machesky

doi:10.1186/1471-2121-6-11

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

Craig F. Stovold, Thomas H. Millard, Laura M. Machesky

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Abstract

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. © 2005 Stovold et al; licensee BioMed Central Ltd.

Original language	English
Journal	BMC Cell Biology
Volume	6
DOIs	https://doi.org/10.1186/1471-2121-6-11
Publication status	Published - 7 Mar 2005

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@article{3e7dcf45035f41a799ce5d810320f79d,

title = "Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2",

abstract = "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. {\textcopyright} 2005 Stovold et al; licensee BioMed Central Ltd.",

author = "Stovold, {Craig F.} and Millard, {Thomas H.} and Machesky, {Laura M.}",

year = "2005",

month = mar,

day = "7",

doi = "10.1186/1471-2121-6-11",

language = "English",

volume = "6",

journal = "BMC Cell Biology",

issn = "1471-2121",

publisher = "Springer Nature",

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T1 - Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2

AU - Stovold, Craig F.

AU - Millard, Thomas H.

AU - Machesky, Laura M.

PY - 2005/3/7

Y1 - 2005/3/7

N2 - 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. © 2005 Stovold et al; licensee BioMed Central Ltd.

AB - 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. © 2005 Stovold et al; licensee BioMed Central Ltd.

U2 - 10.1186/1471-2121-6-11

DO - 10.1186/1471-2121-6-11

M3 - Article

SN - 1471-2121

VL - 6

JO - BMC Cell Biology

JF - BMC Cell Biology

ER -

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

Abstract

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