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- W2060878851 abstract "Bcl-2 exerts its anti-apoptotic effect in part through the regulation of Ca2+ homeostasis at the level of the endoplasmic reticulum. Earlier, we demonstrated that a truncated form of Bcl-2, Bcl-2Δ21, interacts with and destabilizes the skeletal muscle sarco/endoplasmic reticulum Ca-ATPase (SERCA) [Dremina, E. S., Sharov, V. S., Kumar, K., Zaidi, A., Michaelis, E. K., and Schöneich, C. (2004) Biochem. J. 383, 361−370]. Here we show that (i) the transmembrane (TM) domain of Bcl-2 accelerates SERCA inactivation, (ii) both Bcl-2Δ21 and full-length Bcl-2 selectively interact with SERCA1, and (iii) the inactivation of SERCA is accompanied by a translocation of SERCA from caveolae-related domains (CRD) of the sarcoplasmic reticulum (SR). In rat skeletal muscle SR, intact SERCA1 was detected only in the CRD fractions of a sucrose density gradient. Co-incubation of SR with either Bcl-2Δ21 or full-length Bcl-2 resulted in both the appearance of Bcl-2Δ21 or Bcl-2 in the fractions containing SERCA1 and translocation of SERCA1 from CRD fractions; the latter effect correlated with the loss of the Ca-ATPase activity of the protein." @default.
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- W2060878851 date "2005-12-06" @default.
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- W2060878851 title "Displacement of SERCA from SR Lipid Caveolae-Related Domains by Bcl-2: A Possible Mechanism for SERCA Inactivation" @default.
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- W2060878851 doi "https://doi.org/10.1021/bi050800s" @default.
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