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.

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

SBROGGIO', Mauro;FERRETTI, Roberta;ACCORNERO, FEDERICA;TURCO, Emilia;SILENGO, Lorenzo;TARONE, Guido;BRANCACCIO, Mara
2008-01-01

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.
2008
582
1788
1799
http://www.ncbi.nlm.nih.gov/pubmed/?term=The+mammalian+CHORD-containing+protein+melusin+is+a+stress
melusin; HSP90; Annullamento
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.
File in questo prodotto:
File Dimensione Formato  
2008 FEBS.pdf

Accesso riservato

Tipo di file: POSTPRINT (VERSIONE FINALE DELL’AUTORE)
Dimensione 578.07 kB
Formato Adobe PDF
578.07 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/54987
Citazioni
  • ???jsp.display-item.citation.pmc??? 19
  • Scopus 45
  • ???jsp.display-item.citation.isi??? 44
social impact