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Ca 2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane

Ca 2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane,10.1016/j.febslet.2011.10.008,Febs Letters

Ca 2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane  
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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 Ca2+-CaM and TA proteins. Thus, CaM appears to regulate TA insertion into the ER membrane in a Ca2+ dependent manner.
Journal: Febs Letters - FEBS LETT , vol. 585, no. 21, pp. 3485-3490, 2011
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