TY - JOUR
T1 - Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle.
AU - Casella, J. F.
AU - Craig, S. W.
AU - Maack, D. J.
AU - Brown, A. E.
PY - 1987/7
Y1 - 1987/7
N2 - 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.
AB - 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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U2 - 10.1083/jcb.105.1.371
DO - 10.1083/jcb.105.1.371
M3 - Article
C2 - 3301868
AN - SCOPUS:0023372284
SN - 0021-9525
VL - 105
SP - 371
EP - 379
JO - The Journal of cell biology
JF - The Journal of cell biology
IS - 1
ER -