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

doi:10.1016/j.febslet.2011.10.008

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

Division of Molecular & Cellular Function (L5)

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	3485-3490
Number of pages	5
Journal	FEBS Letters
Volume	585
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2011.10.008
Publication status	Published - 4 Nov 2011

Keywords

Calcium
Calmodulin
Membrane insertion
Tail-anchored membrane proteins
Trifluoperazine

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10.1016/j.febslet.2011.10.008

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title = "Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane",

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. {\textcopyright} 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",

keywords = "Calcium, Calmodulin, Membrane insertion, Tail-anchored membrane proteins, Trifluoperazine",

author = "Sarah Ha{\ss}denteufel and Nico Sch{\"a}uble and Patrizia Cassella and Pawel Leznicki and Anika M{\"u}ller and Stephen High and Martin Jung and Richard Zimmermann",

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doi = "10.1016/j.febslet.2011.10.008",

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TY - JOUR

T1 - Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane

AU - Haßdenteufel, Sarah

AU - Schäuble, Nico

AU - Cassella, Patrizia

AU - Leznicki, Pawel

AU - Müller, Anika

AU - High, Stephen

AU - Jung, Martin

AU - Zimmermann, Richard

PY - 2011/11/4

Y1 - 2011/11/4

N2 - 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.

AB - 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.

KW - Calcium

KW - Calmodulin

KW - Membrane insertion

KW - Tail-anchored membrane proteins

KW - Trifluoperazine

UR - https://www.scopus.com/pages/publications/80255129394

U2 - 10.1016/j.febslet.2011.10.008

DO - 10.1016/j.febslet.2011.10.008

M3 - Article

C2 - 22001204

VL - 585

SP - 3485

EP - 3490

JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

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

Abstract

Keywords

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