Molecular and Cellular Biochemistry

, Volume 223, Issue 1, pp 139–145

Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in rabbit fast-twitch muscle sarcoplasmic reticulum

  • Pierangelo Colpo
  • Alessandra Nori
  • Roberta Sacchetto
  • Ernesto Damiani
  • Alfredo Margreth
Article

DOI: 10.1023/A:1017987015807

Cite this article as:
Colpo, P., Nori, A., Sacchetto, R. et al. Mol Cell Biochem (2001) 223: 139. doi:10.1023/A:1017987015807

Abstract

Skeletal muscle triadin is a sarcoplasmic reticulum (SR) membrane protein that had been shown to interact structurally and functionally at the cytoplasmic domain (amino acid residues 1–47) with the ryanodine receptor (RyR1), and to undergo phosphorylation by endogenous calmodulin protein kinase (CaM K II) in isolated terminal cisternae from rabbit fast-twitch muscle. Here we show that triadin cytoplasmic domain expressed as glutathione-S-transferase fusion protein, is a substrate of the protein kinase. This finding is corroborated by identification of a specific consensus sequence in the deduced amino sequence between residue 34 and 37 of triadin. Confirming the regulatory features of CaM K II, we show the phosphorylation of triadin cytoplasmic segment by the kinase, when converted to the autonomous form. We propose that triadin modulates RyR1 in a phosphorylation-dependent manner.

Ca2+-release channel calmodulin protein kinase sarcoplasmic reticulum triadin 

Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • Pierangelo Colpo
    • 1
  • Alessandra Nori
    • 1
  • Roberta Sacchetto
    • 1
  • Ernesto Damiani
    • 1
  • Alfredo Margreth
    • 1
  1. 1.NRC Unit for Muscle Biology and Physiopathology, Department of Experimental Biomedical SciencesUniversity of PadovaPadovaItaly