Journal
GENES & DEVELOPMENT
Volume 26, Issue 2, Pages 114-119Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.177758.111
Keywords
Smyd2; Hsp90; titin; lysine methylation; sarcomere; I-band
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Funding
- Starr Cancer Consortium [13-A136]
- National Institutes of Health [RO1 AI068058, NRSA AI066674, RR00862, RR022220, HL083146, NRSA GM076989]
- German Research Foundation [SFB 629, Li 690/7-2]
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Protein lysine methylation is one of the most widespread post-translational modifications in the nuclei of eukaryotic cells. Methylated lysines on histones and nonhistone proteins promote the formation of protein complexes that control gene expression and DNA replication and repair. In the cytoplasm, however, the role of lysine methylation in protein complex formation is not well established. Here we report that the cytoplasmic protein chaperone Hsp90 is methylated by the lysine methyltransferase Smyd2 in various cell types. In muscle, Hsp90 methylation contributes to the formation of a protein complex containing Smyd2, Hsp90, and the sarcomeric protein titin. Deficiency in Smyd2 results in the loss of Hsp90 methylation, impaired titin stability, and altered muscle function. Collectively, our data reveal a cytoplasmic protein network that employs lysine methylation for the maintenance and function of skeletal muscle.
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