Posttranslational Modifications of Myosin Light Chains Determine the Protein Fate

Cadete, Virgilio J. J.; Sawicki, Grzegorz

doi:10.5772/28656

Cited by 2 publications

(2 citation statements)

References 70 publications

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“…The phosphorylated MLC-2v plays a modulatory role in cardiac torsion, contractility, and myosin stabilization. 32,33 MLCK3 or cardiac myosin light chain kinase 3 (cMLCK), encoded by the mylk3 gene, has been identified in MLC-2v phosphorylation and sarcomere organization. 34 Zebrafish models displayed a considerable downregulation in the transcription and translation of cMLCK proteins in the presence of Dox.…”

Section: Dox and The Cardiac Sarcomere Proteinsmentioning

confidence: 99%

“…Posttranslational modifications in MLC‐2v (nitration, nitrosylation, and phosphorylation) regulate contractility and interactions with the thick filament. The phosphorylated MLC‐2v plays a modulatory role in cardiac torsion, contractility, and myosin stabilization 32,33 . MLCK3 or cardiac myosin light chain kinase 3 (cMLCK), encoded by the mylk3 gene, has been identified in MLC‐2v phosphorylation and sarcomere organization 34 .…”

Section: Effects Of Dox On the Cardiac Regimementioning

confidence: 99%

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A short review: Doxorubicin and its effect on cardiac proteins

Upadhyay

Gupta

Mantha

et al. 2020

J of Cellular Biochemistry

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Doxorubicin (DOX) is a boon for cancer‐suffering patients. However, the undesirable effect on health on vital organs, especially the heart, is a limiting factor, resulting in an increased number of patients with cardiac dysfunction. The present review focuses on the contractile machinery and associated factors, which get affected due to DOX toxicity in chemo‐patients for which they are kept under life‐long investigation for cardiac function. DOX‐induced oxidative stress disrupts the integrity of cardiac contractile muscle proteins that alter the rhythmic mechanism and oxygen consumption rate of the heart. DOX is an oxidant and it is further discussed that oxidative stress prompts the damage of contractile components and associated factors, which include Ca2+ load through Ca2+ ATPase, SERCA, ryanodine receptor‐2, phospholamban, and calsequestrin, which ultimately results in left ventricular ejection and dilation. Based on data and evidence, the associated proteins can be considered as clinical markers to develop medications for patients. Even with the advancement of various diagnosing tools and modified drugs to mitigate DOX‐induced cardiotoxicity, the risk could not be surmounted with survivors of cancer.

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Section: Dox and The Cardiac Sarcomere Proteinsmentioning

confidence: 99%

Section: Effects Of Dox On the Cardiac Regimementioning

confidence: 99%

A short review: Doxorubicin and its effect on cardiac proteins

Upadhyay

Gupta

Mantha

et al. 2020

J of Cellular Biochemistry

View full text Add to dashboard Cite

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First profiling of lysine crotonylation of myofilament proteins and ribosomal proteins in zebrafish embryos

Kwon

Kim

Lee

2018

Sci Rep

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Zebrafish embryos are translucent and develop rapidly in individual eggs ex utero; they are widely used as models for embryogenesis and organ development for human diseases and drug discovery. Lysine crotonylation (Kcr) is a type of histone post-translational modifications discovered in 2011. Kcr dynamics are involved in gene expression regulation and acute kidney injury; however, little is known about the effects of Kcr on non-histone proteins. In the present study, we conducted the first proteome-wide profiling of Kcr in zebrafish larvae and identified 557 Kcr sites on 218 proteins, representing the Kcr event in zebrafish. We identified two types of Kcr motifs containing hydrophobic (Leu, Ile, Val) and acidic (Asp and Glu) amino acids near the modified lysine residues. Our results show that both crotonylated proteins and sites of crotonylation were evolutionarily conserved between zebrafish embryos and humans. Specifically, Kcr on ribosomal proteins and myofilament proteins, including myosin, tropomyosin and troponin, were widely enriched. Interestingly, 55 lysine crotonylation sites on myosin were distributed throughout coiled coil regions. Therefore, Kcr may regulate muscle contraction and protein synthesis. Our results provide a foundation for future studies on the effects of lysine crotonylation on aging and heart failure.

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Posttranslational Modifications of Myosin Light Chains Determine the Protein Fate

Cited by 2 publications

References 70 publications

A short review: Doxorubicin and its effect on cardiac proteins

A short review: Doxorubicin and its effect on cardiac proteins

First profiling of lysine crotonylation of myofilament proteins and ribosomal proteins in zebrafish embryos

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