A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure

Heather K B Simmerman, Yvonne M. Kobayashi, Joseph M. Autry, Larry Jones

Research output: Contribution to journalArticle

216 Citations (Scopus)

Abstract

Phospholamban is a phosphoprotein regulator of cardiac sarcoplasmic reticulum which is phosphorylated in response to β-adrenergic stimulation. Previous results have shown that phospholamban forms Ca2+-selective channels in lipid bilayers. The channel-forming domain has been localized to amino acid residues 26-52, which form a stable pentameric, helical structure. The specific residues responsible for stabilizing the pentameric membrane domain of phospholamban have been identified by mutational analysis. Residues 26-52 were individually mutated to Ala or Phe, and the ability of the resulting mutant to form a pentamer or other oligomer was assessed by SDS- polyacrylamide gel electrophoresis analysis. Replacement of Leu37, Ile40, Leu44, Ile47, or Leu51 by Ala prevented pentamer formation, indicating their essential involvement in the oligomeric assembly. The heptad repeats, and 3-4-residue spacing of the essential amino acids suggest that residues 37-52 adopt a pentameric coiled-coil structure stabilized by a leucine zipper motif formed by the close packing of Leu37, Ile40, Leu44, Ile47, and Leu51. The resulting symmetric structure contains a central pore defined by the hydrophobic surface of the five stabilizing leucine zippers, which are oriented to the interior and form the backbone of the pentamer.

Original languageEnglish
Pages (from-to)5941-5946
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number10
DOIs
StatePublished - Mar 8 1996

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Leucine Zippers
Pore structure
Membranes
Lipid bilayers
Essential Amino Acids
Phosphoproteins
Lipid Bilayers
Sarcoplasmic Reticulum
Electrophoresis
Oligomers
Adrenergic Agents
Polyacrylamide Gel Electrophoresis
Amino Acids
phospholamban

ASJC Scopus subject areas

  • Biochemistry

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A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. / Simmerman, Heather K B; Kobayashi, Yvonne M.; Autry, Joseph M.; Jones, Larry.

In: Journal of Biological Chemistry, Vol. 271, No. 10, 08.03.1996, p. 5941-5946.

Research output: Contribution to journalArticle

Simmerman, Heather K B ; Kobayashi, Yvonne M. ; Autry, Joseph M. ; Jones, Larry. / A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 10. pp. 5941-5946.
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