ArticleThe Journal of biological chemistry2009
Ala scanning of the inhibitory region of cardiac troponin I.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Troponin Revealed: Uncovering the Structure of the Thin Filament On-Off Switch in Striated Muscle.Biophysical journal · 2021Review
- Interplay of actin, ADP and MgArchives of biochemistry and biophysics · 2019Article
- Order-Disorder Transitions in the Cardiac Troponin Complex.Journal of molecular biology · 2016Review
- Molecular and functional consequences of mutations in the central helix of cardiac troponin C.Archives of biochemistry and biophysics · 2014Article
- Cardiac muscle activation blunted by a mutation to the regulatory component, troponin T.The Journal of biological chemistry · 2013Article
- Conserved Asp-137 is important for both structure and regulatory functions of cardiac α-tropomyosin (α-TM) in a novel transgenic mouse model expressing α-TM-D137L.The Journal of biological chemistry · 2013Article
- Perturbed length-dependent activation in human hypertrophic cardiomyopathy with missense sarcomeric gene mutations.Circulation research · 2013Article
- New insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin I.Biochimica et biophysica acta · 2013Article
- Integration of troponin I phosphorylation with cardiac regulatory networks.Circulation research · 2013Review
- Genomic DNA methylation changes in NYGGF4-overexpression 3T3-L1 adipocytes.International journal of molecular sciences · 2012Article
- The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?Biophysical reviews · 2011Review
- Protein phosphorylation and signal transduction in cardiac thin filaments.The Journal of biological chemistry · 2011Review
- Dual regulatory functions of the thin filament revealed by replacement of the troponin I inhibitory peptide with a linker.The Journal of biological chemistry · 2010Article
- Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In skeletal and cardiac muscles, troponin (Tn), which resides on the thin filament, senses a change in intracellular Ca(2+) concentration. Tn is composed of TnC, TnI, and TnT. Ca(2+) binding to the regulatory domain of TnC removes the inhibitory effect by TnI on the contraction. The inhibitory region of cardiac TnI spans from residue 138 to 149. Upon Ca(2+) activation, the inhibitory region is believed to be released from actin, thus triggering actin-activation of myosin ATPase. In this study, we created a series of Ala-substitution mutants of cTnI to delineate the functional contribution of each amino acid in the inhibitory region to myofilament regulation. We found that most of the point mutations in the inhibitory region reduced the ATPase activity in the presence of Ca(2+), which suggests the same region also acts as an activator of the ATPase. The thin filaments can also be activated by strong myosin head (S1)-actin interactions. The binding of N-ethylmaleimide-treated myosin subfragment 1 (NEM-S1) to actin filaments mimics such strong interactions. Interestingly, in the absence of Ca(2+) NEM-S1-induced activation of S1 ATPase was significantly less with the thin filaments containing TnI(T144A) than that with the wild-type TnI. However, in the presence of Ca(2+), there was little difference in the activation of ATPase activity between these preparations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.