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J Biol Chem, Vol. 274, Issue 40, 28466-28475, October 1, 1999
From the Tropomodulin (E-Tmod) is an actin filament
pointed end capping protein that maintains the length of the sarcomeric
actin filaments in striated muscle. Here, we describe the
identification and characterization of a novel tropomodulin isoform,
skeletal tropomodulin (Sk-Tmod) from chickens. Sk-Tmod is 62%
identical in amino acid sequence to the previously described chicken
E-Tmod and is the product of a different gene. Sk-Tmod isoform
sequences are highly conserved across vertebrates and constitute an
independent group in the tropomodulin family. In vitro,
chicken Sk-Tmod caps actin and tropomyosin-actin filament pointed ends
to the same extent as does chicken E-Tmod. However, E- and Sk-Tmods
differ in their tissue distribution; Sk-Tmod predominates in fast
skeletal muscle fibers, lens, and erythrocytes, while E-Tmod is found
in heart and slow skeletal muscle fibers. Additionally, their
expression is developmentally regulated during chicken breast muscle
differentiation with Sk-Tmod replacing E-Tmod after hatching. Finally,
in skeletal muscle fibers that coexpress both Sk- and E-Tmod, they are
recruited to different actin filament-containing cytoskeletal
structures within the cell: myofibrils and costameres, respectively.
All together, these observations support the hypothesis that
vertebrates have acquired different tropomodulin isoforms that play
distinct roles in vivo.
Identification of a Novel Tropomodulin Isoform, Skeletal
Tropomodulin, That Caps Actin Filament Pointed Ends in Fast
Skeletal Muscle
,,,
Department of Cell Biology and the
¶ Skaggs Institute for Chemical Biology, Scripps Research
Institute, La Jolla, California 92037
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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