The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1

FEBS Lett. 2008 Jun 11;582(13):1788-94. doi: 10.1016/j.febslet.2008.04.058. Epub 2008 May 12.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Gene Expression Profiling
  • Gene Expression Regulation
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / metabolism*
  • Immunoprecipitation
  • Mice
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Muscle Proteins / genetics
  • Muscle Proteins / metabolism*
  • Protein Structure, Tertiary


  • Adaptor Proteins, Signal Transducing
  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • HSP90 Heat-Shock Proteins
  • Itgb1bp2 protein, mouse
  • Molecular Chaperones
  • Muscle Proteins
  • Sugt1 protein, mouse