Domain:The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.,Function:Potent inhibitor of cell death. Isoform Bcl-X(L) anti-apoptotic activity is inhibited by association with SIVA isoform 1. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channnel (VDAC) by binding to it and preventing the release of the caspase activator, cytochrome c, from the mitochondrial membrane. The Bcl-X(S) isoform promotes apoptosis.,PTM:Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity.,similarity:Belongs to the Bcl-2 family.,subcellular location:Mitochondrial membranes and perinuclear envelope.,subunit:Bcl-X(L) forms homodimers, and heterodimers with BAX, BAK and BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Also interacts with BAD and BBC3. Isoform Bcl-X(L) binds to Siva isoform 1. Interacts with BCL2L11 (By similarity). Interacts with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with BAX isoform Sigma.,tissue specificity:Bcl-X(S) is expressed at high levels in cells that undergo a high rate of turnover, such as developing lymphocytes. In contrast, Bcl-X(L) is found in tissues containing long-lived postmitotic cells, such as adult brain.,
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