Calmodulin interacts with the cytoplasmic tails of the parathyroid hormone 1 receptor and a sub-set of class b G-protein coupled receptors

FEBS Lett. 2005 Jan 31;579(3):803-7. doi: 10.1016/j.febslet.2004.12.056.

Abstract

Parathyroid hormone (PTH) binds to its receptor (PTH 1 receptor, PTH1R) and activates multiple pathways. The PTH1R, a class b GPCR, contains consensus calmodulin-binding motifs. The PTH1R cytoplasmic tail interacts with calmodulin in a calcium-dependent manner via the basic 1-5-8-14 motif. Calcium-dependent calmodulin interactions with the cytoplasmic tails of receptors for PTH 2, vasoactive intestinal peptide, pituitary adenylate cyclase activating peptide, corticotropin releasing hormone, calcitonin, and the glucagon-like peptides 1 and 2 are demonstrated. The cytoplasmic tails of the secretin receptor and the growth hormone releasing hormone receptor either interact poorly or not at all with calmodulin, respectively. Fluphenazine, a calmodulin antagonist, enhances PTH-mediated accumulation of total inositol phosphates, suggesting that calmodulin regulates signaling via phospholipase C.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Calmodulin / metabolism*
  • Cell Line
  • Cytoplasm / metabolism*
  • Humans
  • Immunohistochemistry
  • Molecular Sequence Data
  • Point Mutation
  • Receptor, Parathyroid Hormone, Type 1 / chemistry
  • Receptor, Parathyroid Hormone, Type 1 / genetics
  • Receptor, Parathyroid Hormone, Type 1 / metabolism*
  • Receptors, G-Protein-Coupled / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • Calmodulin
  • Receptor, Parathyroid Hormone, Type 1
  • Receptors, G-Protein-Coupled