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Cap Z(36/32), a Barbed End Actin-capping Protein, is a Component of the Z-line of Skeletal Muscle

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1987 Jul 1
PMID 3301868
Citations 56
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Abstract

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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References
1.
Maher P, Cox G, Singer S . Zeugmatin: a new high molecular weight protein associated with Z lines in adult and early embryonic striated muscle. J Cell Biol. 1985; 101(5 Pt 1):1871-83. PMC: 2113980. DOI: 10.1083/jcb.101.5.1871. View

2.
Schleicher M, Gerisch G, Isenberg G . New actin-binding proteins from Dictyostelium discoideum. EMBO J. 1984; 3(9):2095-100. PMC: 557648. DOI: 10.1002/j.1460-2075.1984.tb02096.x. View

3.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

4.
Yin H, Zaner K, Stossel T . Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation. J Biol Chem. 1980; 255(19):9494-500. View

5.
Tseng P, Pollard T . Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2. J Cell Biol. 1982; 94(1):213-8. PMC: 2112199. DOI: 10.1083/jcb.94.1.213. View