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Trends Mol Med. 2019 Jun 21. pii: S1471-4914(19)30125-X. doi: 10.1016/j.molmed.2019.05.008. [Epub ahead of print]

Shaping Striated Muscles with Ubiquitin Proteasome System in Health and Disease.

Author information

1
INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Toulouse, France. Electronic address: karim.hnia@inserm.frkarim.hnia@inserm.fr.
2
Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Campus-Vienna-Biocenter 1, 1030, Vienna, Austria; Medical University of Vienna, Vienna BioCenter (VBC), 1030, Vienna, Austria.
3
Institut de Pharmacologie et de Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France. Electronic address: Christel.Lutz@ipbs.frChristel.Lutz@ipbs.fr.

Abstract

For long-lived contractile cells, such as striated muscle cells, maintaining proteome integrity is a challenging task. These cells require hundreds of components that must be properly synthesized, folded, and incorporated into the basic contractile unit, the sarcomere. Muscle protein quality control in cells is mainly guaranteed by the ubiquitin-proteasome system (UPS), the lysosome-autophagy system, and various molecular chaperones. Recent studies establish the concept of dedicated UPS in the regulation of sarcomere assembly during development and in adult life to maintain the intricate and interwoven organization of protein complexes in muscle. Failure of sarcomere protein quality control often represents the basis of severe myopathies and cardiomyopathies in human, further highlighting its importance in producing and maintaining the contractile machinery of muscle cells in shape.

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