A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics.

@article{Raskin2012ANM,
  title={A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics.},
  author={Anna M Raskin and Stephan Lange and Katherine Banares and Robert C. Lyon and Anke Zieseniss and Leonard K. Lee and Katrina Go Yamazaki and Henk L. M. Granzier and Carol C. Gregorio and Andrew D. McCulloch and Jeffrey H. Omens and Farah Sheikh},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 35},
  pages={
          29273-84
        }
}
Understanding mechanisms underlying titin regulation in cardiac muscle function is of critical importance given recent compelling evidence that highlight titin mutations as major determinants of human cardiomyopathy. We previously identified a cardiac biomechanical stress-regulated complex at the cardiac-specific N2B region of titin that includes four-and-a-half LIM domain protein-1 (Fhl1) and components of the mitogen-activated protein signaling cascade, which impacted muscle compliance in… CONTINUE READING

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