S-Palmitoylation and S-Oleoylation of Rabbit and Pig Sarcolipin

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Cédric Montigny, CNRS - CEA - Université Paris Sud, France;
  • ,
  • Paulette Decottignies, CNRS - Université Paris Sud, France;
  • ,
  • Pierre le Maréchal, CNRS - Université Paris Sud, France;, Unknown
  • Pierre Capy, CNRS - Université Paris Sud, France;, Unknown
  • Maike Bublitz, Danish National Research Foundation, Aarhus University, Denmark., Denmark
  • Claus Olesen
  • Jesper Vuust Møller
  • Marc le Maire, CNRS - CEA - Université Paris Sud, France; marc.lemaire@cea.fr.
  • ,
  • Poul Nissen

Sarcolipin (SLN) is a regulatory peptide present in sarcoplasmic reticulum (SR) from skeletal muscle of animals. We find that native rabbit SLN is modified by a fatty acid anchor on Cys9 with a palmitic acid in about 60% and, surprisingly, an oleic acid in the remaining 40%. SLN used for co-crystallization with SERCA1a (1) is also palmitoylated/oleoylated, but is not visible in crystal structures, probably due to disorder. Treatment with 1 M hydroxylamine for 1 hour removes the fatty acids from a majority of the SLN pool. This treatment did not modify the SERCA1a affinity for Ca2+ but increased the Ca2+-dependent ATPase activity of SR membranes indicating that the S-acylation of SLN or of other proteins is required for this effect on SERCA1a. Pig SLN is also fully palmitoylated/oleoylated on its Cys9 residue, but in a reverse ratio of about 40/60. An alignment of 67 SLN sequences from the protein databases shows that 19 of them contain a cysteine and the rest a phenylalanine at position 9. Based on a cladogram we postulate that the mutation from phenylalanine to cysteine in some species is the result of an evolutionary convergence. We suggest that, besides phosphorylation, S-acylation/deacylation also regulates SLN activity.

Original languageEnglish
JournalJournal of Biological Chemistry
Volume289
Pages (from-to)33850-33861
Number of pages12
ISSN0021-9258
DOIs
Publication statusPublished - 5 Dec 2014

    Research areas

  • Calcium ATPase, Mass Spectrometry (MS), Membrane Protein, Protein Acylation, Protein Palmitoylation, Sarcoplasmic Reticulum (SR), Protein Oleoylation, Sarcolipin

See relations at Aarhus University Citationformats

ID: 83544843