There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum

There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum Proteins of the Bcl-2 family are important regulators of cell fate. The role of these proteins in controlling mitochondrial apoptotic processes has been extensively investigated, although exact molecular mechanisms are incompletely understood. However, mounting evidence indicates that these proteins also function at the endoplasmic reticulum and other locations within the cell. Both pro- and anti-apoptotic Bcl-2 family members can regulate endoplasmic reticulum calcium, cellular pH and endoplasmic reticulum resident proteins. In this review, we discuss the activities and potential targets of Bcl-2 family members at the endoplasmic reticulum and other cellular locations. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochimica et Biophysica Acta (BBA) - Molecular Cell Research Elsevier

There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum

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Publisher
Elsevier
Copyright
Copyright © 2003 Elsevier B.V.
ISSN
0167-4889
D.O.I.
10.1016/j.bbamcr.2003.07.001
Publisher site
See Article on Publisher Site

Abstract

Proteins of the Bcl-2 family are important regulators of cell fate. The role of these proteins in controlling mitochondrial apoptotic processes has been extensively investigated, although exact molecular mechanisms are incompletely understood. However, mounting evidence indicates that these proteins also function at the endoplasmic reticulum and other locations within the cell. Both pro- and anti-apoptotic Bcl-2 family members can regulate endoplasmic reticulum calcium, cellular pH and endoplasmic reticulum resident proteins. In this review, we discuss the activities and potential targets of Bcl-2 family members at the endoplasmic reticulum and other cellular locations.

Journal

Biochimica et Biophysica Acta (BBA) - Molecular Cell ResearchElsevier

Published: Mar 1, 2004

References

  • The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
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  • Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2
    He, H.; Lam, M.; McCormick, T.S.; Distelhorst, C.W.
  • Effects of PMCA and SERCA pump overexpression on the kinetics of cell Ca(2+) signalling
    Brini, M.; Bano, D.; Manni, S.; Rizzuto, R.; Carafoli, E.
  • The Ca 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action
    Pinton, P.; Ferrari, D.; Rapizzi, E.; Di Virgilio, F.D.; Pozzan, T.; Rizzuto, R.
  • Movement of Bax from the cytosol to mitochondria during apoptosis
    Wolter, K.G.; Hsu, Y.T.; Smith, C.L.; Nechushtan, A.; Xi, X.G.; Youle, R.J.
  • Conformation of the Bax C-terminus regulates subcellular location and cell death
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  • Regulated targeting of BAX to mitochondria
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  • p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    Ng, F.W.; Nguyen, M.; Kwan, T.; Branton, P.E.; Nicholson, D.W.; Cromlish, J.A.; Shore, G.C.
  • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
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