MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains (Q24290468)

apoptotic signaling pathway

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BCL2-associated X protein

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Modulator of apoptosis 1

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author name string

K O Tan

1

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K M Tan

2

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S L Chan

3

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K S Yee

4

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M Bevort

5

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K C Ang

6

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V C Yu

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

26 January 2001

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published in

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volume

276

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issue

4

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page(s)

2802-7

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cites work

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Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2

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

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

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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

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F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosis

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The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells.

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Isolation and characterization of a novel member of the neural zinc finger factor/myelin transcription factor family with transcriptional repression activity

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Gene identification using the yeast two-hybrid system.

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1-(5-Isoquinolinesulfonyl)-2-methylpiperazine induces apoptosis in human neuroblastoma cells, SH-SY5Y, through a p53-dependent pathway

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Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells

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Ma1, a novel neuron- and testis-specific protein, is recognized by the serum of patients with paraneoplastic neurological disorders

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A serologic marker of paraneoplastic limbic and brain-stem encephalitis in patients with testicular cancer

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Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations

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Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

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BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity

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Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing

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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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BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites

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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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BID: a novel BH3 domain-only death agonist

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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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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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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Modulation of cell death in yeast by the Bcl-2 family of proteins.

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Mitochondria and apoptosis

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

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Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation

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Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1

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Bcl-xL does not inhibit the function of Apaf-1.

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

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A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity

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

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Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases

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