Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit is collaboration with pro-apoptotic Bak or Bax (Q77870361)

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8 December 2019

title

Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit is collaboration with pro-apoptotic Bak or Bax (English)

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8 December 2019

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3

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8 December 2019

author name string

Arlette B Werner

1

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8 December 2019

Evert de Vries

2

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8 December 2019

Ilja Bontjer

4

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8 December 2019

Jannie Borst

5

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8 December 2019

language of work or name

English

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publication date

19 April 2002

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Journal of Biological Chemistry

8 December 2019

published in

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8 December 2019

volume

277

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8 December 2019

issue

25

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8 December 2019

page(s)

22781-22788

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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

8 December 2019

cites work

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Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

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Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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Mitochondria as the central control point of apoptosis

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GRS, a novel member of the Bcl-2 gene family, is highly expressed in multiple cancer cell lines and in normal leukocytes

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The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis

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Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis

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NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes

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A1 expression is stimulated by CD40 in B cells and rescues WEHI 231 cells from anti-IgM-induced cell death

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NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis

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BH3-Only proteins-essential initiators of apoptotic cell death

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Endothelial cell death induced by tumor necrosis factor-alpha is inhibited by the Bcl-2 family member, A1

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A1 functions at the mitochondria to delay endothelial apoptosis in response to tumor necrosis factor

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Functional dissection of Bfl-1, a Bcl-2 homolog: anti-apoptosis, oncogene-cooperation and cell proliferation activities

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Accelerated neutrophil apoptosis in mice lacking A1-a, a subtype of the bcl-2-related A1 gene.

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Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells

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Bcl-2-family proteins: the role of the BH3 domain in apoptosis

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PUMA induces the rapid apoptosis of colorectal cancer cells

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PUMA, a novel proapoptotic gene, is induced by p53

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Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis

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BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak

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Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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Conformation of the Bax C-terminus regulates subcellular location and cell death

21 January 2018

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis

21 January 2018

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Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis

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Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells

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BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis

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Identifiers

DOI

10.1074/JBC.M201469200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11929871%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

1 reference