Structural perspectives of phospholamban, a helical transmembrane pentamer

Isaiah T. Arkin*, Paul D. Adams, Axel T. Brünger, Steven O. Smith, Donald M. Engelman

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

60 Scopus citations

Abstract

Phospholamban is a 52-amino-acid protein that assembles into a pentamer in sarcoplasmic reticulum membranes. The protein has a role in the regulation of the resident calcium ATPase through an inhibitory association that can be reversed by phosphorylation. The phosphorylation of phospholamban is initiated by β-adrenergic stimulation, identifying phospholamban as an important component in the stimulation of cardiac activity by β-agonists. It is this role of phospholamban that has motivated studies in recent decades. There is evidence that phospholamban may also function as a Ca2+-selective ion channel. The structural properties of phospholamban have been studied by mutagenesis, modeling, and spectroscopy, resulting in a new view of the organization of this key molecule in membranes.

Original languageAmerican English
Pages (from-to)157-179
Number of pages23
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume26
DOIs
StatePublished - 1997
Externally publishedYes

Keywords

  • Calcium regulation
  • Ion channel
  • Membrane protein
  • Sarcoplasmic reticulum
  • Transmembrane helices

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