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Binding of a native titin fragment to actin is regulated by PIP2
Author(s) -
Astier Catherine,
Raynaud Fabrice,
Lebart Marie-Christine,
Roustan Claude,
Benyamin Yves
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00572-9
Subject(s) - titin , obscurin , actin , myofibril , chemistry , biophysics , fragment (logic) , biochemistry , microbiology and biotechnology , sarcomere , biology , myocyte , computer science , programming language
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.