ArticleJournal of structural biology2010
The effects of PKCalpha phosphorylation on the extensibility of titin's PEVK element.
Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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
24 citing papers in PubMed, 42 citations in OpenAlex.
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- Protein Kinase C Family: Structures, Biological Functions, Diseases, and Pharmaceutical Interventions.MedComm · 2025Review
- Novel Drug Targets in Diastolic Heart Disease.International journal of molecular sciences · 2025Review
- Glycerol storage increases passive stiffness of muscle fibers through effects on titin extensibility.The Journal of general physiology · 2025Article
- Effects of Eccentric Speed during Front Squat Conditioning Activity on Post-activation Performance Enhancement of Hip and Thigh Muscles.Journal of human kinetics · 2024Article
- Titin (TTN): from molecule to modifications, mechanics, and medical significance.Cardiovascular research · 2022Review
- The titin N2B and N2A regions: biomechanical and metabolic signaling hubs in cross-striated muscles.Biophysical reviews · 2021Review
- Posttranslational modifications of titin from cardiac muscle: how, where, and what for?The FEBS journal · 2019Review
- Characterization of biventricular alterations in myocardial (reverse) remodelling in aortic banding-induced chronic pressure overload.Scientific reports · 2019Article
- The multiple roles of titin in muscle contraction and force production.Biophysical reviews · 2018Review
- Cardiomyocytes Sense Matrix Rigidity through a Combination of Muscle and Non-muscle Myosin Contractions.Developmental cell · 2018Article
- Right Ventricular Myocardial Stiffness in Experimental Pulmonary Arterial Hypertension: Relative Contribution of Fibrosis and Myofibril Stiffness.Circulation. Heart failure · 2016Article
- Phosphorylating Titin's Cardiac N2B Element by ERK2 or CaMKIIδ Lowers the Single Molecule and Cardiac Muscle Force.Biophysical journal · 2015Article
- Increased myocardial stiffness due to cardiac titin isoform switching in a mouse model of volume overload limits eccentric remodeling.Journal of molecular and cellular cardiology · 2015Article
- Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Cardiac titin and heart disease.Journal of cardiovascular pharmacology · 2014Review
- Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium.European biophysics journal : EBJ · 2013Article
- Titin is a major human disease gene.Circulation · 2013Review
- Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Biophysical journal · 2013Article
- The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements.Journal of molecular and cellular cardiology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Post-translational modifications, along with isoform splicing, of titin determine the passive tension development of stretched sarcomeres. It was recently shown that PKCalpha phosphorylates two highly-conserved residues (S26 and S170) of the PEVK region in cardiac titin, resulting in passive tension increase. To determine how each phosphorylated residue affects myocardial stiffness, we generated three recombinant mutant PEVK fragments (S26A, S170A and S170A/S26A), each flanked by Ig domains. Single-molecule force spectroscopy shows that PKCalpha decreases the PEVK persistence length (from 0.99 to 0.68 nm); the majority of this decrease is attributable to phosphorylation of S26. Before PKCalpha, all three mutant PEVK fragments showed at least 40% decrease in persistence length compared to wildtype. Furthermore, Ig domain unfolding force measurements indicate that PEVK's flanking Ig domains are relatively unstable compared to other titin Ig domains. We conclude that phosphorylation of S26 is the primary mechanism through which PKCalpha modulates cardiac stiffness.
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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.