Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization
| Autor: | Alexander Tarakhovsky, Carol C. Gregorio, Andreas Unger, Christopher T. Pappas, Steffen Just, Wolfgang Rottbauer, Wolfgang A. Linke, Laura T. Donlin, Brian T. Chait, Marc-Werner Dobenecker, Erica Y. Jacobs, Martina Krüger, Christian Andresen, Anke Zieseniss, Tobias Voelkel, Eugene Rudensky |
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| Rok vydání: | 2012 |
| Předmět: |
Cytoplasm
Methyltransferase Lysine Muscle Proteins Chick Embryo Methylation complex mixtures Research Communication 03 medical and health sciences 0302 clinical medicine Non-histone protein Myofibrils polycyclic compounds Genetics Animals Humans Connectin HSP90 Heat-Shock Proteins Muscle Skeletal Zebrafish 030304 developmental biology 0303 health sciences biology Myocardium Histone-Lysine N-Methyltransferase Recombinant Proteins Histone Biochemistry Histone methyltransferase Chaperone (protein) biology.protein bacteria Titin Protein Kinases 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Genes & Development. 26:114-119 |
| ISSN: | 1549-5477 0890-9369 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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