FEBS Letters
Volume 582, Issue 13 , Pages 1788-1794, 11 June 2008

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

Edited by Felix Wieland

  • Mauro Sbroggiò

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Roberta Ferretti

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Elena Percivalle

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Malgorzata Gutkowska

      Affiliations

    • International Institute of Molecular and Cell Biology in Warsaw, 4 Trojdena Street, Warsaw, Poland
    • Nencki Institute of Experimental Biology, Warsaw, Poland
    • ,
  • Alicja Zylicz

      Affiliations

    • International Institute of Molecular and Cell Biology in Warsaw, 4 Trojdena Street, Warsaw, Poland
    • ,
  • Wojciech Michowski

      Affiliations

    • International Institute of Molecular and Cell Biology in Warsaw, 4 Trojdena Street, Warsaw, Poland
    • Nencki Institute of Experimental Biology, Warsaw, Poland
    • ,
  • Jacek Kuznicki

      Affiliations

    • International Institute of Molecular and Cell Biology in Warsaw, 4 Trojdena Street, Warsaw, Poland
    • Nencki Institute of Experimental Biology, Warsaw, Poland
    • ,
  • Federica Accornero

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Beniamina Pacchioni

      Affiliations

    • CRIBI Biotechnology Centre and Biology Department, University of Padova, Padova, Italy
    • ,
  • Gerolamo Lanfranchi

      Affiliations

    • CRIBI Biotechnology Centre and Biology Department, University of Padova, Padova, Italy
    • ,
  • Jorg Hamm

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Emilia Turco

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Lorenzo Silengo

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Guido Tarone

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • ,
  • Mara Brancaccio

      Affiliations

    • Department of Genetics, Biology and Biochemistry, University of Torino, Molecular Biotechnology Center, via Nizza, 52, Torino, Italy
    • Corresponding Author InformationCorresponding author. Fax: +39 116706432.

Received 8 January 2008; received in revised form 27 March 2008; accepted 14 April 2008. published online 12 May 2008.

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.

Structured summary


MINT-6538515:melusin (Q9R000)physically interacts (MI:0218) with Hsp90 (P07901) by anti bait co-immunoprecipitation (MI:0006)

MINT-6538566, MINT-6538556:Hsp90 (P07901) physically interacts (MI:0218) with melusin (Q9R000) by cross-linking studies (MI:0030)

MINT-6538524:melusin (Q9R000) physically interacts (MI:0218) with Sgt1 (Q9CS74) by anti tag co-immunoprecipitation (MI:0007)

MINT-6538595:Hsp90 (P07901) physically interacts (MI:0218) with melusin (Q9R000) by enzyme linked immunosorbent assay (MI:0411)

MINT-6538543:melusin (Q9R000) physically interacts (MI:0218) with Sgt1 (Q9CS74) by anti bait co-immunoprecipitation (MI:0006)

MINT-6538580: melusin (Q9R000) physically interacts (MI:0218) with Hsp90 (P07901) by surface plasmon resonance (MI:0107)

Keywords: Melusin, CHORD containing proteins, Hsp90, Sgt1

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PII: S0014-5793(08)00397-9

doi:10.1016/j.febslet.2008.04.058

FEBS Letters
Volume 582, Issue 13 , Pages 1788-1794, 11 June 2008

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