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Vol. 11, Issue 11, 3805-3817, November 2000
and
*Department of Medicine, The Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205; and The ~80-kDa erythroid 4.1R protein is a major component of the
erythrocyte cytoskeleton, where it links transmembrane proteins to the
underlying spectrin/actin complexes. A diverse collection of 4.1R
isoforms has been described in nonerythroid cells, ranging from ~30
to ~210 kDa. In the current study, we identified the number and
primary structure of 4.1R isoforms expressed in adult skeletal muscle
and characterized the localization patterns of 4.1R message and
protein. Skeletal muscle 4.1R appears to originate solely from the
upstream translation initiation codon (AUG-1) residing in exon 2'.
Combinations of alternatively spliced downstream exons generate an
array of distinct 4.1R spliceoforms. Two major isoform classes of
~105/110 and ~135 kDa are present in muscle homogenates. 4.1R
transcripts are distributed in highly ordered signal stripes, whereas
4.1R protein(s) decorate the sarcoplasm in transverse striations that
are in register with A-bands. An ~105/110-kDa 4.1R isoform appears to
occur in vivo in a supramolecular complex with major sarcomeric
proteins, including myosin, Department of
Molecular Biology and Genetics, The Johns Hopkins University,
Baltimore, Maryland 21205
-actin, and -tropomyosin. In vitro
binding assays showed that 4.1R may interact directly with the
aforementioned contractile proteins through its 10-kDa domain. All of
these observations suggest a topological model whereby 4.1R may play a
scaffolding role by anchoring the actomyosin myofilaments and possibly
modulating their displacements during contraction/relaxation.
Corresponding author. E-mail address:
schuang{at}welch.jhu.edu.
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