Interaction of nebulin SH3 domain with titin PEVK and myopalladin: Implications for the signaling and assembly role of titin and nebulin

Kan Ma, Kuan Wang

研究成果: 雜誌貢獻文章同行評審

58 引文 斯高帕斯(Scopus)

摘要

Skeletal muscle nebulin is thought to determine thin filament length and regulate actomyosin interaction in a calcium/calmodulin or S100 sensitive manner. We have investigated the binding of nebulin SH3 with proline-rich peptides derived from the 28-mer PEVK modules of titin and the Z-line protein myopalladin, using fluorescence, circular dichroism and nuclear magnetic resonance techniques. Of the six peptides studied, PR2 of titin (VPEKKAPVAPPK) and myopalladin MyoP2 (646VKEPPPVLAKPK657) bind to nebulin SH3 with micromolar affinity (∼31 and 3.4 μM, respectively), whereas the other four peptides bind weakly (>100 μM). Sequence analysis of titins reveals numerous SH3 binding motifs that are highly enriched in the PEVK segments of titin isoforms. Our findings suggest that titin PEVK and myopalladin may play signaling roles in targeting and orientating nebulin to the Z-line during sarcomere assembly.

原文英語
頁(從 - 到)273-278
頁數6
期刊FEBS Letters
532
發行號3
DOIs
出版狀態已發佈 - 十二月 18 2002
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學

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