Bcl-2-family proteins: the role of the BH3 domain in apoptosis. (Q47686942)

4 February 2018

review article

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title

Bcl-2-family proteins: the role of the BH3 domain in apoptosis. (English)

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4 February 2018

main subject

BH4 domain binding

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Kelekar A

1

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4 February 2018

Thompson CB

series ordinal

2

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4 February 2018

publication date

1 August 1998

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4 February 2018

published in

Trends in Cell Biology

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4 February 2018

volume

8

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4 February 2018

issue

8

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4 February 2018

page(s)

324-330

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4 February 2018

The central executioners of apoptosis: caspases or mitochondria?

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C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2.

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Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members

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Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL

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BID: a novel BH3 domain-only death agonist

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Bim: a novel member of the Bcl-2 family that promotes apoptosis

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harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)

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Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist

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Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2.

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The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4

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Functional dissection of the human Bc12 protein: sequence requirements for inhibition of apoptosis

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Bcl-2 functions in an antioxidant pathway to prevent apoptosis

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Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

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Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c

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Multiple Bcl-2 family members demonstrate selective dimerizations with Bax

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BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax.

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Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

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Bcl-x(L) forms an ion channel in synthetic lipid membranes.

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Comparison of the ion channel characteristics of proapoptotic BAX and antiapoptotic BCL-2.

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Channel formation by antiapoptotic protein Bcl-2.

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Inhibition of Bax channel-forming activity by Bcl-2

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7 January 2021

Mitochondrial control of nuclear apoptosis.

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Mitochondrial permeability transition is a central coordinating event of apoptosis

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The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis

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Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked

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Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria

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Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL.

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Functional dissection of the pro-apoptotic protein Bik. Heterodimerization with anti-apoptosis proteins is insufficient for induction of cell death

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Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death

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Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

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Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death

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Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

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Interaction and regulation of subcellular localization of CED-4 by CED-9

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Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex

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7 January 2021

Regulation of apoptosis by BH3 domains in a cell-free system

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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7 January 2021

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Identifiers

DOI

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4 February 2018

PubMed ID

9704409

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4 February 2018