ArticlePloS one2014
Protein kinase C phosphomimetics alter thin filament Ca2+ binding properties.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 16 citations in OpenAlex.
- Mouse Models of Cardiomyopathies Caused by Mutations in Troponin C.International journal of molecular sciences · 2023Review
- Article
- Computational Methods Elucidate Consequences of Mutations and Post-translational Modifications on Troponin I Effective Concentration to Troponin C.The journal of physical chemistry. B · 2021Article
- Cardiac contractile dysfunction and protein kinase C-mediated myofilament phosphorylation in disease and aging.The Journal of general physiology · 2019Article
- Troponin I modulation of cardiac performance: Plasticity in the survival switch.Archives of biochemistry and biophysics · 2019Review
- The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform.Expert review of proteomics · 2017Review
- Functional communication between PKC-targeted cardiac troponin I phosphorylation sites.Archives of biochemistry and biophysics · 2017Article
- Restrictive Cardiomyopathy Troponin I R145W Mutation Does Not Perturb Myofilament Length-dependent Activation in Human Cardiac Sarcomeres.The Journal of biological chemistry · 2016Article
- Functionally conservative substitutions at cardiac troponin I S43/45.Archives of biochemistry and biophysics · 2016Article
- Designing proteins to combat disease: Cardiac troponin C as an example.Archives of biochemistry and biophysics · 2016Review
- Interplay between the effects of a Protein Kinase C phosphomimic (T204E) and a dilated cardiomyopathy mutation (K211Δ or R206W) in rat cardiac troponin T blunts the magnitude of muscle length-mediated crossbridge recruitment against the β-myosin heavy chain background.Journal of muscle research and cell motility · 2016Article
- Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I.Frontiers in physiology · 2016Article
- Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration.Frontiers in physiology · 2016Article
- Independent modulation of contractile performance by cardiac troponin I Ser43 and Ser45 in the dynamic sarcomere.Journal of molecular and cellular cardiology · 2015Article
- Tri-modal regulation of cardiac muscle relaxation; intracellular calcium decline, thin filament deactivation, and cross-bridge cycling kinetics.Biophysical reviews · 2014Article
- Cardiac troponin I tyrosine 26 phosphorylation decreases myofilament Ca2+ sensitivity and accelerates deactivation.Journal of molecular and cellular cardiology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Adrenergic stimulation modulates cardiac function by altering the phosphorylation status of several cardiac proteins. The Troponin complex, which is the Ca(2+) sensor for cardiac contraction, is a hot spot for adrenergic phosphorylation. While the effect of β-adrenergic related PKA phosphorylation of troponin I at Ser23/24 is well established, the effects of α-adrenergic induced PKC phosphorylation on multiple sites of TnI (Ser43/45, Thr144) and TnT (Thr194, Ser198, Thr203 and Thr284) are much less clear. By utilizing an IAANS labeled fluorescent troponin C, TnC(IAANS)(T53C), we systematically examined the site specific effects of PKC phosphomimetic mutants of TnI and TnT on TnC's Ca(2+) binding properties in the Tn complex and reconstituted thin filament. The majority of the phosphomemetics had little effect on the Ca(2+) binding properties of the isolated Tn complex. However, when incorporated into the thin filament, the phosphomimetics typically altered thin filament Ca(2+) sensitivity in a way consistent with their respective effects on Ca(2+) sensitivity of skinned muscle preparations. The altered Ca(2+) sensitivity could be generally explained by a change in Ca(2+) dissociation rates. Within TnI, phosphomimetic Asp and Glu did not always behave similar, nor were Ala mutations (used to mimic non-phosphorylatable states) benign to Ca(2+) binding. Our results suggest that Troponin may act as a hub on the thin filament, sensing physiological stimuli to modulate the contractile performance of the heart.
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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.