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Cell Calcium. 2011 Sep;50(3):251-60. doi: 10.1016/j.ceca.2011.05.005. Epub 2011 Jun 12.

The ancient cell death suppressor BAX inhibitor-1.

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  • 1Neurologische Klinik, Universitätsklinikum Düsseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany.

Abstract

Bax inhibitor-1 (BI-1) was initially identified for its ability to inhibit BAX-induced apoptosis in yeast cells and is the founding member of a family of highly hydrophobic proteins localized in diverse cellular membranes. It is evolutionarily conserved and orthologues from plants can substitute for mammalian BI-1 in regard to its anti-apoptotic function suggesting a high degree of functional conservation. BI-1 interacts with BCL-2 and BCL-XL and, similar to these two anti-apoptotic proteins, the effect of BI-1 on cell death involves changes in the amount of Ca(2+) releasable from intracellular stores. However, BI-1 is also a negative regulator of the endoplasmic reticulum stress sensor IRE1 α, it interacts with G-actin and increases actin polymerization, enhances cancer metastasis by altering glucose metabolism and activating the sodium-hydrogen exchanger, and reduces the production of reactive oxygen species through direct interaction with NADPH-P450 reductase. In this contribution, we summarize what is known about the expression, intracellular localization and structure of BI-1 and specifically illuminate its effects on the intracellular Ca(2+) homeostasis and how this might relate to its other functions. We also present a thorough phylogenetic analysis of BI-1 proteins from major phyla together with paralogues from all BI-1 family members.

Copyright © 2011 Elsevier Ltd. All rights reserved.

PMID:
21663964
[PubMed - indexed for MEDLINE]
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