The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1 |
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Authors: | Sbroggiò Mauro Ferretti Roberta Percivalle Elena Gutkowska Malgorzata Zylicz Alicja Michowski Wojciech Kuznicki Jacek Accornero Federica Pacchioni Beniamina Lanfranchi Gerolamo Hamm Jorg Turco Emilia Silengo Lorenzo Tarone Guido Brancaccio Mara |
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Affiliation: | Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy. |
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Abstract: | Melusin is a mammalian muscle specific CHORD containing protein capable of activating signal transduction pathways leading to cardiomyocytes hypertrophy in response to mechanical stress. To define melusin function we searched for molecular partners possibly involved in melusin dependent signal transduction. Here we show that melusin and heat shock proteins are co-regulated. Moreover, melusin directly binds to Hsp90, a ubiquitous chaperone involved in regulating several signaling pathways. In addition, melusin interacts with Sgt1, an Hsp90 binding molecule. Melusin does not behave as an Hsp90 substrate but rather as a chaperone capable to protect citrate synthase from heat induced aggregation. These results describe melusin as a new component of the Hsp90 chaperone machinery. |
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Keywords: | Melusin CHORD containing proteins Hsp90 Sgt1 |
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