ArticleBiophysical journal2008
The cardiac Ca2+-sensitive regulatory switch, a system in dynamic equilibrium.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Desensitization of the Cardiac Troponin Complex by TnI Phosphorylation and Epigallocatechin-3-Gallate.ACS omega · 2026Article
- The molecular basis for diminished muscle function in acidosis: a proposal.Journal of muscle research and cell motility · 2020Article
- CaBiophysical journal · 2018Article
- Dynamic Equilibrium of Cardiac Troponin C's Hydrophobic Cleft and Its Modulation by CaBioconjugate chemistry · 2017Article
- Probing the mechanism of cardiovascular drugs using a covalent levosimendan analog.Journal of molecular and cellular cardiology · 2016Article
- Regulatory domain of troponin moves dynamically during activation of cardiac muscle.Journal of molecular and cellular cardiology · 2014Article
- In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation.Biophysical journal · 2014Article
- Kinetics of fast changing intramolecular distance distributions obtained by combined analysis of FRET efficiency kinetics and time-resolved FRET equilibrium measurements.Biophysical journal · 2014Article
- Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges.Archives of biochemistry and biophysics · 2013Article
- Kinetic mechanism of Ca²⁺-controlled changes of skeletal troponin I in psoas myofibrils.Biophysical journal · 2012Article
- Functional effects of a restrictive-cardiomyopathy-linked cardiac troponin I mutation (R145W) in transgenic mice.Journal of molecular biology · 2009Article
- Ala scanning of the inhibitory region of cardiac troponin I.The Journal of biological chemistry · 2009Article
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3 authors.
Funding
Abstract
The Ca(2+)-sensitive regulatory switch of cardiac muscle is a paradigmatic example of protein assemblies that communicate ligand binding through allosteric change. The switch is a dimeric complex of troponin C (TnC), an allosteric sensor for Ca(2+), and troponin I (TnI), an allosteric reporter. Time-resolved equilibrium Förster resonance energy transfer (FRET) measurements suggest that the switch activates in two steps: a TnI-independent Ca(2+)-priming step followed by TnI-dependent opening. To resolve the mechanistic role of TnI in activation we performed stopped-flow FRET measurements of activation after rapid addition of a lacking component (Ca(2+) or TnI) and deactivation after rapid chelation of Ca(2+). Time-resolved measurements, stopped-flow measurements, and Ca(2+)-titration measurements were globally analyzed in terms of a new quantitative dynamic model of TnC-TnI allostery. The analysis provided a mesoscopic parameterization of distance changes, free energy changes, and transition rates among the accessible coarse-grained states of the system. The results reveal that 1), the Ca(2+)-induced priming step, which precedes opening, is the rate-limiting step in activation; 2), closing is the rate-limiting step in de-activation; 3), TnI induces opening; 4), there is an incompletely deactivated population when regulatory Ca(2+) is not bound, which generates an accessory pathway of activation; and 5), there is incomplete activation by Ca(2+)-when regulatory Ca(2+) is bound, a 3:2 mixture of dynamically interconverting open (active) and primed-closed (partially active) conformers is observed (15 degrees C). Temperature-dependent stopped-flow FRET experiments provide a near complete thermokinetic parameterization of opening: the enthalpy change (DeltaH = -33.4 kJ/mol), entropy change (DeltaS = -0.110 kJ/mol/K), heat capacity change (DeltaC(p) = -7.6 kJ/mol/K), the enthalpy of activation (delta(double dagger) = 10.6 kJ/mol) and the effective barrier crossing attempt frequency (nu(adj) = 1.8 x 10(4) s(-1)).
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