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Titin-like kinases form mechanosensory signaling nodes central to myofibril regulation, exhibiting diverse mechanisms of activation, scaffolding interactions, and catalytic properties across species.
This review highlights the evolutionary and functional diversity of titin-like kinases as central mechanosensory signaling nodes in muscle.
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Diversity of titin-like kinases extends mechanosensory models in muscle; leaves open clinical relevance in cardiomyopathy pending human validation.
The giant cytoskeletal kinases of the titin-like family are emerging as key mediators of stretch-sensing in muscle. It is thought that their elastic conformational deformation during muscle function regulates both their catalysis and the recruitment of regulatory proteins to signalosomes that assemble in their vicinity. In the present article, we discuss the speciation of mechanosensory mechanisms in titin-like kinases, their scaffolding properties and the kinase/pseudokinase domain variations that define a rich functional diversity across the family.
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Mayans et al. (2013) conducted a review in Muscle mechanosensing. Titin-like kinases was evaluated. Titin-like kinases form mechanosensory signaling nodes central to myofibril regulation, exhibiting diverse mechanisms of activation, scaffolding interactions, and catalytic properties across species.
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