Binding of a native titin fragment to actin is regulated by PIP2

FEBS Letters

Raynaud, Fabrice¹  Benyamin, Yves¹  Lebart, Marie-Christine¹  Roustan, Claude¹  Astier, Catherine¹ 

[1] Laboratoire de Motilité Cellulaire EPHE, UMR 5539, Université des Sciences et Techniques du Languedoc, Place Eugène Bataillon, 34090 Montpellier, France

关键词: Muscle structure;    Titin;    Thin filament;    Actin polymerization;    Phosphoinositide;    ELISA;    enzyme-linked immunosorbent assay;    F-actin;    filamentous actin;    G-actin;    globular actin;    GPI;    glycerophosphomyoinositol;    PI;    phosphatidylinositol;    PIP2;    phosphatidyl inositol 4;    5-biphosphate;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(98)00572-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Titin is a giant protein which extends from Z-line to M-line in striated muscles. We report here the purification of a 150-kDa titin fragment, obtained after V8 protease treatment of myofibrils. This polypeptide was located at the N1-line level, in a titin part known to exhibit stiff properties correlated to an association with actin. By solid or liquid phase binding assays and cosedimentation, we have clearly demonstrated a direct, saturable and relative high affinity binding of the native titin fragment to F-actin. The 150-kDa titin fragment was also shown to accelerate actin polymerization. Furthermore, the actin-titin interaction was found to be inhibited by phosphoinositides.

【 授权许可】

Unknown