The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon

S.B. Marston; C.S. Redwood

doi:10.1016/S0021-9258(18)31391-7

Journal Article| Volume 268, ISSUE 17, P12317-12320, June 15, 1993

The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon

S.B. Marston
S.B. Marston
Affiliations
Department of Cardiac Medicine, National Heart and Lung Institute, London, United Kingdom.
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C.S. Redwood
C.S. Redwood
Affiliations
Department of Cardiac Medicine, National Heart and Lung Institute, London, United Kingdom.
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Open AccessPublished:June 15, 1993DOI:https://doi.org/10.1016/S0021-9258(18)31391-7

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We compared the mechanisms by which caldesmon inhibits actin and actin-tropomyosin activation of myosin subfragment 1 (S1) MgATPase activity. Caldesmon always inhibited actin activation by displacing S1.ADP.Pi from actin and inhibition required at least 0.7 caldesmon molecules bond per actin for 90% inhibition. Caldesmon inhibited actin-tropomyosin without any displacement of S1.ADP.Pi; thus it inhibits a rate-limiting step. Inhibition is highly cooperative, requiring no more than one caldesmon bound per 10 actins for 90% inhibition of activation by actin and smooth muscle tropomyosin. The degree of cooperativity is defined by the tropomyosin since inhibition by skeletal tropomyosin requires up to one caldesmon bound per 4 actins for 90% inhibition under identical conditions. Both noncooperative inhibition of actin and cooperative, tropomyosin-dependent, inhibition are manifested by a fragment of caldesmon containing only the C-terminal 99 amino acids (658C), although this fragment does not itself bind to tropomyosin. The functional properties of 658C are very similar to striated muscle troponin I, consequently we propose a similar mechanism for tropomyosin-dependent regulation by caldesmon. Caldesmon binding switches actin-tropomyosin to the “off” or “weak” state and Ca2+/calmodulin binding to caldesmon blocks this switch and thus reactivates the actin filament.

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Published online: June 15, 1993

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The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon

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