Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin

FEBS Letters

Mues, Alexander¹  Gautel, Mathias¹  Young, Paul¹  Fürst, Dieter O²  van der Ven, Peter F.M² 

[1] Structural Biology Division, European Molecular Biology Laboratory, Meyerhofstr 1, 69117 Heidelberg, Germany;Department for Cell Biology, University of Potsdam, Lennéstr. 7a, 14471 Potsdam, Germany

关键词: Titin;    Connectin;    Telethonin;    Z-disk;    Myofibrillogenesis;   

DOI  :  10.1016/S0014-5793(98)00501-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The giant muscle protein titin/connectin plays a crucial role in myofibrillogenesis as a molecular ruler for sarcomeric protein sorting. We describe here that the N-terminal titin immunoglobulin domains Z1 and Z2 interact specifically with telethonin in yeast two-hybrid analysis and protein binding assays. Immunofluorescence with antibodies against the N-terminal region of titin and telethonin detects both proteins at the Z-disc of human myotubes. Longer titin fragments, comprising a serine-proline-rich phosphorylation site and the next domain, do not interact. The interaction of telethonin with titin is therefore conformation-dependent, reflecting a possible phosphorylation regulation during myofibrillogenesis.

【 授权许可】

Unknown