Sequence analysis of the ryanodine receptor: possible association with a 12K, FK506-binding immunophilin/protein kinase C inhibitor

Biochem Biophys Res Commun. 1991 Aug 15;178(3):1288-90. doi: 10.1016/0006-291x(91)91033-9.

Abstract

A computer-assisted sequence analysis of the ryanodine receptor pointed to a 15-residue peptide, "KC7", reported to have been purified from a proteolytic digest of the 565 kDa rabbit skeletal muscle protein. Sequence comparisons, however, showed that this peptide probably originated from a much smaller protein which copurified with the ryanodine receptor. Peptide KC7 (excluding its unknown N-terminal residue) was identical to the N-terminus of a 12 kDa immunophilin (immunosupressant-binding protein), human T-cell FK506- binding protein (FKBP), which has recently been identified as an inhibitor of protein kinase C. There was no other sequence similarity between FKBP and the ryanodine receptor. It is suggested that in vivo interaction of the ryanodine receptor and FKBP may play a role in the modulation of calcium release in muscle.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / genetics*
  • Databases, Factual
  • Humans
  • Immunosuppressive Agents / metabolism
  • Molecular Sequence Data
  • Muscles / metabolism
  • Protein Kinase C / antagonists & inhibitors*
  • Rabbits
  • Receptors, Cholinergic / genetics*
  • Ryanodine / metabolism
  • Ryanodine Receptor Calcium Release Channel
  • Sequence Homology, Nucleic Acid
  • T-Lymphocytes / immunology
  • Tacrolimus Binding Proteins

Substances

  • Carrier Proteins
  • Immunosuppressive Agents
  • Receptors, Cholinergic
  • Ryanodine Receptor Calcium Release Channel
  • Ryanodine
  • Protein Kinase C
  • Tacrolimus Binding Proteins