Recombinant Mouse Apoptosis regulator Bcl-2 (Bcl2), partial

Function

Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785)

Subcellular Location

Mitochondrion outer membrane (Single-pass membrane protein); Nucleus membrane (Single-pass membrane protein); Endoplasmic reticulum membrane (Single-pass membrane protein); Cytoplasm

Tissue Specificity

Expressed in a variety of tissues

Subunit

Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (By similarity). Component of the complex, at least composed of LRPPRC, BECN1 and BCL2; the interactions prevent BECN1 from forming an autophagy-inducing complex with PIK3C3 (By similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts (via the BH4 domain) with EGLN3; the interaction prevents the formation of the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2 (By similarity). Interacts with EI24. Interacts with G0S2; this interaction also prevents the formation of the anti-apoptotic BAX-BCL2 complex. Interacts with PPIF; the interaction is impaired by CsA (By similarity). Interacts with BOP (By similarity). Interacts with the SCF(FBXO10) complex (By similarity). Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats) (By similarity). Interacts with GIMAP3/IAN4 and GIMAP4/IAN1 (PubMed:16509771). Also interacts with GIMAP5/IAN5 (PubMed:16509771, PubMed:21502331). Interacts with BCAP31 (By similarity). Interacts with IRF3 (By similarity). Interacts with BECN1; thereby inhibiting autophagy in non-starvation conditions (By similarity). Interacts with AMBRA1; thereby inhibiting autophagy (By similarity)

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• Mural R.J. et al. PubMed: CI-70VOHH7BF94TO (JUL-)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
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• Deng X. et al. Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. — J. Biol. Chem. (1998)
• Zhao X. et al. Apoptosis factor EI24/PIG8 is a novel endoplasmic reticulum-localized Bcl-2-binding protein which is associated with suppression of breast cancer invasiveness. — Cancer Res. (2005)