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Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (...
Formato: | Texto |
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Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1987
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114938/ https://www.ncbi.nlm.nih.gov/pubmed/3301868 |
Sumario: | Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (Casella, J. F., D. J. Maack, and S. Lin, 1986, J. Biol. Chem., 261:10915-10921) is localized to the barbed ends of actin filaments by electron microscopy and to the Z-line of chicken skeletal muscle by indirect immunofluorescence and electron microscopy. Since actin filaments associate with the Z-line at their barbed ends, these findings suggest that Cap Z(36/32) may play a role in regulating length, orienting, or attaching actin filaments to Z-discs. |
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