Muscle-Specific RING Finger (MuRF) cDNAs in Atlantic Salmon (Salmo salar) and Their Role as Regulators of Muscle Protein Degradation

L. Tacchi, C.J. Secombes, R. Bickerdike, S.A.M. Martin

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

The selection of proteins destined for degradation by the ubiquitin-proteasome pathway is coordinated by E3 ubiquitin ligases (E3Ub). One group of E3Ubs is described as muscle-specific RING finger (MuRF) molecules. In mammals, these proteins are believed to be central to targetting of muscle proteins for degradation during physiological perturbations such as starvation and inflammatory responses. In fish, the diversity of MuRF sequences is unexplored as is the expression of their mRNAs. In this study, three MuRF1 cDNAs, denoted as MuRF1a, MuRF1b, and MuRF1c, and a single MuRF2 were identified and characterized in Atlantic salmon. The MuRF1 sequences are highly conserved and encode predicted proteins of 349, 350, and 353 amino acids, whereas MuRF2 encodes a longer protein of 462 amino acids. The evolutionary relationship of these sequences with other fish and mammalian molecules shows that MuRF1a and 1b may have arisen from a recent salmonid duplication. The mRNA of MuRFs was expressed in multiple tissues, with highest abundance in white muscle tissue followed by the heart. The expression of MuRFs was modulated after both starvation and immune challenge. Starvation increased expression of all MuRF mRNAs in white muscle, with the greatest increase found in MuRF1a. A proinflammatory stimulation increased expression of MuRF mRNA in muscle and other tissues indicating a role of these proteins in protein degradation during inflammation.
Original languageEnglish
Pages (from-to)35-45
Number of pages11
JournalMarine Biotechnology
Volume14
Issue number1
DOIs
Publication statusPublished - 1 Jan 2011

Keywords

  • Atlantic salmon
  • proteasome
  • MuRF1
  • MuRF2
  • protein degradation
  • E3 ubiquitin ligase

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