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.
Skip Nav Destination
Article navigation
1 July 1987
Article|
July 01 1987
Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle.
J F Casella
S W Craig
D J Maack
A E Brown
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1987) 105 (1): 371–379.
Citation
J F Casella, S W Craig, D J Maack, A E Brown; Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle.. J Cell Biol 1 July 1987; 105 (1): 371–379. doi: https://doi.org/10.1083/jcb.105.1.371
Download citation file:
Sign in
Don't already have an account? Register
Client Account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your Institution
Sign in via your InstitutionSuggested Content
Email alerts
Advertisement
Advertisement