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

Mauro Sbroggiò, Roberta Ferretti, Elena Percivalle, Malgorzata Gutkowska, Alicja Zylicz, Wojciech Michowski, Jacek Kuznicki, Federica Accornero, Beniamina Pacchioni, Gerolamo Lanfranchi, Jorg Hamm, Emilia Turco, Lorenzo Silengo, Guido Tarone, Mara Brancaccio

Research output: Contribution to journalArticle

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).

Original languageEnglish
Pages (from-to)1788-1794
Number of pages7
JournalFEBS Letters
Volume582
Issue number13
DOIs
Publication statusPublished - Jun 11 2008

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Signal transduction
Heat-Shock Proteins
Immunoprecipitation
Citrate (si)-Synthase
Immunosorbents
Signal Transduction
Surface plasmon resonance
Machinery
Muscle
Assays
Mechanical Stress
Proteins
Agglomeration
Surface Plasmon Resonance
Cardiac Myocytes
Hypertrophy
Molecules
Substrates
Enzymes
Hot Temperature

Keywords

  • CHORD containing proteins
  • Hsp90
  • Melusin
  • Sgt1

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Sbroggiò, M., Ferretti, R., Percivalle, E., Gutkowska, M., Zylicz, A., Michowski, W., ... Brancaccio, M. (2008). The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1. FEBS Letters, 582(13), 1788-1794. https://doi.org/10.1016/j.febslet.2008.04.058

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

In: FEBS Letters, Vol. 582, No. 13, 11.06.2008, p. 1788-1794.

Research output: Contribution to journalArticle

Sbroggiò, M, Ferretti, R, Percivalle, E, Gutkowska, M, Zylicz, A, Michowski, W, Kuznicki, J, Accornero, F, Pacchioni, B, Lanfranchi, G, Hamm, J, Turco, E, Silengo, L, Tarone, G & Brancaccio, M 2008, 'The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1', FEBS Letters, vol. 582, no. 13, pp. 1788-1794. https://doi.org/10.1016/j.febslet.2008.04.058
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. / The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1. In: FEBS Letters. 2008 ; Vol. 582, No. 13. pp. 1788-1794.
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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. 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).",
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AU - Sbroggiò, Mauro

AU - Ferretti, Roberta

AU - Percivalle, Elena

AU - Gutkowska, Malgorzata

AU - Zylicz, Alicja

AU - Michowski, Wojciech

AU - Kuznicki, Jacek

AU - Accornero, Federica

AU - Pacchioni, Beniamina

AU - Lanfranchi, Gerolamo

AU - Hamm, Jorg

AU - Turco, Emilia

AU - Silengo, Lorenzo

AU - Tarone, Guido

AU - Brancaccio, Mara

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N2 - 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).

AB - 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).

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