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Vol. 13, Issue 7, 2347-2359, July 2002


and
*Department of Physiology, University of Maryland School of
Medicine, Baltimore, Maryland 21201; and The sarcolemma of fast-twitch muscle is organized into
"costameres," structures that are oriented transversely, over the Z and M lines of nearby myofibrils, and longitudinally, to form a
rectilinear lattice. Here we examine the role of desmin, the major
intermediate filament protein of muscle in organizing costameres. In
control mouse muscle, desmin is enriched at the sarcolemmal domains
that lie over nearby Z lines and that also contain
Department of
Cell Biology, Baylor College of Medicine, Houston, Texas 77030
-spectrin. In
tibialis anterior muscle from mice lacking desmin due to homologous recombination, most costameres are lost. In myofibers from desmin
/
quadriceps, by contrast, most costameric structures are stable. Alternatively, Z line domains may be lost, whereas domains oriented longitudinally or lying over M lines are retained. Experiments with
pan-specific antibodies to intermediate filament proteins and to
cytokeratins suggest that control and desmin
/
muscles express
similar levels of cytokeratins. Cytokeratins concentrate at the
sarcolemma at all three domains of costameres when the latter are
retained in desmin
/
muscle and redistribute with
-spectrin at
the sarcolemma when costameres are lost. Our results suggest that
desmin associates with and selectively stabilizes the Z line domains of
costameres, but that cytokeratins associate with all three domains of
costameres, even in the absence of desmin.
Present address: Department of Cell and Structural
Biology, University of Illinois, Urbana, IL 61801.
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