Caldesmon: binding to actin and myosin and effects on elementary steps in the ATPase cycle

Citation
Jm. Chalovich et al., Caldesmon: binding to actin and myosin and effects on elementary steps in the ATPase cycle, ACT PHYSL S, 164(4), 1998, pp. 427-435
Citations number
59
Categorie Soggetti
Physiology
Journal title
ACTA PHYSIOLOGICA SCANDINAVICA
ISSN journal
00016772 → ACNP
Volume
164
Issue
4
Year of publication
1998
Pages
427 - 435
Database
ISI
SICI code
0001-6772(199812)164:4<427:CBTAAM>2.0.ZU;2-9
Abstract
The actin binding protein caldesmon inhibits the actin-activation of myosin ATPase activity. The steps in the cycle of ATP hydrolysis that caldesmon c ould inhibit include: (1) the binding of myosin to actin, (2) the transitio n between any two actin-myosin states and (3) the distribution between inac tive and active states of actin. The analysis of these possibilities is com plicated because caldesmon binds to both myosin and actin and because each caldesmon molecule binds to several actin monomers. This paper reviews proc edures for analysing these interactions and summarizes current information on the stability and dynamics of the interaction of caldesmon with actin an d myosin. Possible effects of caldesmon on transitions within the ATPase cy cle of actomyosin are also discussed.