The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms
Open accessAbstract
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), 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 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.
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Citations
Cites
Control of nonmuscle myosins by phosphorylation
Tan, J. L., Ravid, S., & Spudich, J. A. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003445 · Cited by 353
Cited by
ADF/Cofilin: a functional node in cell biology
Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704
Self-citationTropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space
Gunning, P., O’neill, G., & Hardeman, E. (2008) · Physiological Reviews · doi:10.1152/physrev.00001.2007 · Cited by 478
Self-citationCytoskeletal and signaling mechanisms of neurite formation
Sainath, R., & Gallo, G. (2015) · Cell and Tissue Research · doi:10.1007/s00441-014-1955-0 · Cited by 116
Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms
Selvaraj, M., Kokate, S. B., Reggiano, G., Kogan, K., Kotila, T., Kremneva, E., DiMaio, F., Lappalainen, P., & Huiskonen, J. T. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111900 · Cited by 22
Metadata
- Authors
- Bryce, N. S., Schevzov, G., Ferguson, V., Percival, J. M., Lin, J. J.-C., Matsumura, F., Bamburg, J. R., Jeffrey, P. L., Hardeman, E. C., Gunning, P., & Weinberger, R. P.
- Venue
- Molecular Biology of the Cell
- Published
- 2003-03
- Volume
- 14
- Issue
- 3
- Pages
- 1002-1016
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2149966352
- Cited by
- 242
- References
- 1
- FWCI
- 3.57
- Type
- journal article
- Language
- en
- Open access
- green
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- Bryce, N. S., Schevzov, G., Ferguson, V., Percival, J. M., Lin, J. J.-C., Matsumura, F., Bamburg, J. R., Jeffrey, P. L., Hardeman, E. C., Gunning, P., & Weinberger, R. P. (2003). Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e02-04-0244
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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