Specification of actin filament function and molecular composition by tropomyosin isoforms

被引:192
作者
Bryce, NS
Schevzov, G
Ferguson, V
Percival, JM
Lin, JJC
Matsumura, F
Bamburg, JR
Jeffrey, PL
Hardeman, EC
Gunning, P
Weinberger, RP [1 ]
机构
[1] Univ Sydney, Dept Paediat & Child Hlth, Oncol Res Unit, Childrens Hosp Westmead, Westmead, NSW 2145, Australia
[2] Childrens Med Res Inst, Muscle Dev Unit, Westmead, NSW 2145, Australia
[3] Childrens Med Res Inst, Dev Neurobiol Unit, Westmead, NSW 2145, Australia
[4] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA
[5] Rutgers State Univ, Dept Mol Biol & Biochem, Nelson Labs, Piscataway, NJ USA
[6] Univ Iowa, Dept Biol Sci, Iowa City, IA USA
关键词
D O I
10.1091/mbc.E02-04-0244
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5(NM1))1 to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape. hTm5(NM1) was able to recruit myosin 11 into stress fibers, which resulted in decreased lamellipodia and cellular migration. In contrast, TmBr3 transfection induced lamellipodial formation, increased cellular migration, and reduced stress fibers. Based on coimmunoprecipitation and colocalization studies, TmBr3 appeared to be associated with actin-depolymerizing factor/cofilin (ADF)-bound actin filaments. Additionally, the Tms can specifically regulate the incorporation of other Tms into actin filaments, suggesting that selective dimerization may also be involved in the control of actin filament organization. We conclude that Tm isoforms can be used to specify the functional properties and molecular composition of actin filaments and that spatial segregation of isoforms may lead to localized specialization of actin filament function.
引用
收藏
页码:1002 / 1016
页数:15
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