Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression

Bin Yang, Oxana Ibraghimov-Beskrovnaya, Carolyn R. Moomaw, Clive A. Slaughter, Kevin P. Campbell

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107 Scopus citations


The 59-kDa dystrophin-associated protein triplet (59-DAP) is a component of the dystrophin-glycoprotein complex which may directly associate with dystrophin. The cDNA encoding one component (59-1 DAP) of the 59-DAP triplet has now been cloned from rabbit skeletal muscle. The deduced amino acid sequence of 59-1 DAP predicts a 505-amino acid polypeptide containing nine potential phosphorylation sites and no predicted transmembrane domains. This is consistent with the 59-1 DAP being a peripheral membrane protein associated with the cytoplasmic face of the dystrophin-glycoprotein complex. Affinity-purified antibodies against rabbit 59-1 DAP fusion proteins only recognize the lowest band of the 59-DAP triplet in skeletal muscle sarcolemma and isolated dystrophin-glycoprotein complex. The tissue-specific expression of 59-1 DAP mRNA, which is most prominent in skeletal and cardiac muscle and is also detected in brain, parallels that of dystrophin but not of utrophin. Levels of 59-1 DAP mRNA are unaffected in mdx mouse skeletal and cardiac muscles, although all dystrophin-associated proteins, including 59-DAP, are greatly reduced in mdx mouse skeletal muscle. However, in mdx mouse cardiac muscle, the up-regulation of utrophin preserves all dystrophin-associated proteins except 59-DAP. Our results suggest that the 59-DAP triplet may contain different protein species and that the 59-1 DAP may associate more specifically with dystrophin than with utrophin.

Original languageEnglish (US)
Pages (from-to)6040-6044
Number of pages5
JournalJournal of Biological Chemistry
Issue number8
StatePublished - Feb 25 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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