ArticleCell motility and the cytoskeleton2009
Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit.
Article in Cell motility and the cytoskeleton, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.
- Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation.Frontiers in physiology · 2022Pooled it
- Novel Protein Production Method Combining Native Expression in Human Cells with an Intein-based Affinity Purification and Self-cleavable Tag.Bio-protocol · 2022Article
- Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins.The Journal of biological chemistry · 2021Article
- Acidosis modifies effects of phosphorylated tropomyosin on the actin-myosin interaction in the myocardium.Journal of muscle research and cell motility · 2021Article
- Quantitative proteomic and phosphoproteomic profiling of ischemic myocardial stunning in swine.American journal of physiology. Heart and circulatory physiology · 2020Article
- Tropomyosin pseudo-phosphorylation results in dilated cardiomyopathy.The Journal of biological chemistry · 2019Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- HCM and DCM cardiomyopathy-linked α-tropomyosin mutations influence off-state stability and crossbridge interaction on thin filaments.Archives of biochemistry and biophysics · 2018Article
- Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Molecular and cellular neurosciences · 2017Review
- Direct measurement of cortical force generation and polarization in a living parasite.Molecular biology of the cell · 2017Article
- Clinically Divergent Mutation Effects on the Structure and Function of the Human Cardiac Tropomyosin Overlap.Biochemistry · 2017Article
- Muscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres.Human molecular genetics · 2015Article
- A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.PLoS computational biology · 2015Article
- Phosphorylation of Ser283 enhances the stiffness of the tropomyosin head-to-tail overlap domain.Archives of biochemistry and biophysics · 2015Article
- Modifications of myofilament protein phosphorylation and function in response to cardiac arrest induced in a swine model.Frontiers in physiology · 2015Article
- Loop 2 of myosin is a force-dependent inhibitor of the rigor bond.Journal of muscle research and cell motility · 2014Article
- Tropomyosin de-phosphorylation in the heart: what are the consequences?Journal of muscle research and cell motility · 2013Review
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.Archives of biochemistry and biophysics · 2013Article
- Post-translational modifications of myofilament proteins involved in length-dependent prolongation of relaxation in rabbit right ventricular myocardium.Archives of biochemistry and biophysics · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tropomyosin (Tm) is one of the major phosphoproteins comprising the thin filament of muscle. However, the specific role of Tm phosphorylation in modulating the mechanics of actomyosin interaction has not been determined. Here we show that Tm phosphorylation is necessary for long-range cooperative activation of myosin binding. We used a novel optical trapping assay to measure the isometric stall force of an ensemble of myosin molecules moving actin filaments reconstituted with either natively phosphorylated or dephosphorylated Tm. The data show that the thin filament is cooperatively activated by myosin across regulatory units when Tm is phosphorylated. When Tm is dephosphorylated, this "long-range" cooperative activation is lost and the filament behaves identically to bare actin filaments. However, these effects are not due to dissociation of dephosphorylated Tm from the reconstituted thin filament. The data suggest that end-to-end interactions of adjacent Tm molecules are strengthened when Tm is phosphorylated, and that phosphorylation is thus essential for long range cooperative activation along the thin filament.
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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.