Functional differences between the N-terminal domains of mouse and human myosin binding protein-C

Samantha - Harris, Justin F. Shaffer, Peony Wong, Kristina L. Bezold

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The N-terminus of cMyBP-C can activate actomyosin interactions in the absence of Ca2+, but it is unclear which domains are necessary. Prior studies suggested that the Pro-Ala rich region of human cMyBP-C activated force in permeabilized human cardiomyocytes, whereas the C1 and M-domains of mouse cMyBP-C activated force in permeabilized rat cardiac trabeculae. Because the amino acid sequence of the P/A region differs between human and mouse cMyBP-C isoforms (46% identity), we investigated whether species-specific differences in the P/A region could account for differences in activating effects. Using chimeric fusion proteins containing combinations of human andmouse C0, Pro-Ala, and C1 domains, we demonstrate here that the human P/A and C1 domains activate actomyosin interactions, whereas the same regions of mouse cMyBP-C are less effective. These results suggest that species-specific differences between homologous cMyBP-C isoforms confer differential effects that could fine-tune cMyBP-C function in hearts of different species.

Original languageEnglish (US)
Article number789798
JournalJournal of Biomedicine and Biotechnology
Volume2010
DOIs
StatePublished - 2010
Externally publishedYes

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Actomyosin
Protein Isoforms
Rats
Fusion reactions
Amino Acids
Proteins
Cardiac Myocytes
Amino Acid Sequence
myosin-binding protein C

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Medicine
  • Genetics
  • Molecular Biology
  • Health, Toxicology and Mutagenesis
  • Medicine(all)

Cite this

Functional differences between the N-terminal domains of mouse and human myosin binding protein-C. / Harris, Samantha -; Shaffer, Justin F.; Wong, Peony; Bezold, Kristina L.

In: Journal of Biomedicine and Biotechnology, Vol. 2010, 789798, 2010.

Research output: Contribution to journalArticle

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