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Originally published as MBC in Press, 10.1091/mbc.E02-04-0244 on December 7, 2002
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Vol. 14, Issue 3, 1002-1016, March 2003

Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms

Nicole S. Bryce,* Galina Schevzov,* Vicki Ferguson,* Justin M. Percival,* Jim J.-C. Lin,dagger Fumio Matsumura,Dagger James R. Bamburg,§ Peter L. Jeffrey, Edna C. Hardeman,|| Peter Gunning,* and Ron P. Weinberger*#@

 *Oncology Research Unit, Department of Paediatrics and Child Health, University of Sydney, The Children's Hospital at Westmead, Westmead NSW 2145, Australia;  dagger Department of Biological Sciences, The University of Iowa, Iowa City, Iowa;  Dagger Department of Molecular Biology and Biochemistry, Rutgers University, Nelson Labs, Busch Campus, Piscataway, New Jersey;  §Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado; and  Developmental Neurobiology and  ||Muscle Development Units, Children's Medical Research Institute, Westmead, NSW 2145, Australia

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 (hTM5NM1), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape. hTm5NM1 was able to recruit myosin II 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.

# Corresponding author. E-mail address: Ron.Weinberger{at}proteomesystems.com.au.

@ Present address: Proteome Systems, Ltd., North Ryde, New South Wales Z670, Australia.

Molecular Biology of the Cell
Vol. 14, 1002-1016, March 2003
Copyright © 2003 by The American Society for Cell Biology


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