Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane

Sarah Haßdenteufel, Nico Schäuble, Patrizia Cassella, Pawel Leznicki, Anika Müller, Stephen High, Martin Jung, Richard Zimmermann

Research output: Contribution to journalArticlepeer-review

Abstract

Cytosolic components and pathways have been identified that are involved in inserting tail-anchored (TA) membrane proteins into the yeast or mammalian endoplasmic reticulum (ER) membrane. Searching for regulatory mechanisms of TA protein biogenesis, we found that Ca2+-calmodulin (CaM) inhibits the insertion of TA proteins into mammalian ER membranes and that this inhibition is prevented by trifluoperazine, a CaM antagonist that interferes with substrate binding of Ca2+-CaM. The effects of Ca2+-CaM on cytochrome b5 and Synaptobrevin 2 suggest a direct interaction between Ca 2+-CaM and TA proteins. Thus, CaM appears to regulate TA insertion into the ER membrane in a Ca2+ dependent manner. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)3485-3490
Number of pages5
JournalFEBS Letters
Volume585
Issue number21
DOIs
Publication statusPublished - 4 Nov 2011

Keywords

  • Calcium
  • Calmodulin
  • Membrane insertion
  • Tail-anchored membrane proteins
  • Trifluoperazine

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