Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT

Biochemistry
Tamatha BaxleyJ M Chalovich

Abstract

Striated muscle contraction is regulated by the actin-associated proteins tropomyosin and troponin. The extent of activation of myosin ATPase activity is lowest in the absence of both Ca2+ and activating cross-bridges (i.e., S1-ADP or rigor S1). Binding of activating species of myosin to actin at a saturating Ca2+ concentration stabilizes the most active state (M state) of the actin-tropomyosin-troponin complex (regulated actin). Ca2+ binding alone produces partial stabilization of the active state. The extent of stabilization at a saturating Ca2+ concentration depends on the isoform of the troponin subunits, the phosphorylation state of troponin, and, in the case of cardiac muscle, the presence of hypertrophic cardiomyopathy-producing mutants of troponin T and troponin I. Cardiac dysfunction is also associated with mutations of troponin C (TnC). Troponin C mutants A8V, C84Y, and D145E increase the Ca2+ sensitivity of ATPase activity. We show that these mutants change the distribution of regulated actin states. The A8V and C84Y TnC mutants decreased the inactive B state distribution slightly at low Ca2+ concentrations, but the D145E mutants had no effect on that state. All TnC mutants increased the level of the active M state c...Continue Reading

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Citations

Aug 21, 2020·Acta Neuropathologica Communications·Joshua S ClaytonKristen J Nowak
Apr 9, 2020·Frontiers in Physiology·Alfredo Jesus López-DávilaRobert Stehle

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