Displacement of Serca from Sr Lipid Caveolae-related Domains by Bcl-2: a Possible Mechanism for Serca Inactivation.
From: Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047, USA.
Biochemistry
- Publish Date: Jan 2006
- ISSN: 0006-2960
- Volume: 45
- Issue: 1
- Pages: 175-84
- Medium: Print
- Language: English
- Citation (JAMA): Dremina Elena S, Sharov Victor S, Schöneich Christian, et al. Displacement of Serca from Sr Lipid Caveolae-related Domains by Bcl-2: a Possible Mechanism for Serca Inactivation.. Biochemistry Jan 2006;45:175-84
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-2delta21, 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-2delta21 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-2delta21 or full-length Bcl-2 resulted in both the appearance of Bcl-2delta21 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.
Mesh Headings (Keywords): Animals, Calcium-Transporting ATPases, Caveolae, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Muscle, Skeletal, Protein Binding, Protein Conformation, Protein Folding, Proto-Oncogene Proteins c-bcl-2, Rats, Sarcoplasmic Reticulum, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Time Factors
Check for Full Text / PubMed Unique Identifier (PMID): 16388593
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