Title : Mcl-1 interacts with truncated Bid and inhibits its induction of cytochrome c release and its role in receptor-mediated apoptosis.

Pub. Date : 2006 Mar 3

PMID : 16380381






3 Functional Relationships(s)
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1 Here, we have identified the anti-apoptotic Bcl-2 family member Mcl-1 as a potent tBid-binding partner. tBID BCL2 apoptosis regulator Homo sapiens
2 Site-directed mutagenesis reveals that the Bcl-2 homology (BH)3 domain of tBid is essential for binding to Mcl-1, whereas all three BH domains (BH1, BH2, and BH3) of Mcl-1 are required for interaction with tBid. tBID BCL2 apoptosis regulator Homo sapiens
3 Site-directed mutagenesis reveals that the Bcl-2 homology (BH)3 domain of tBid is essential for binding to Mcl-1, whereas all three BH domains (BH1, BH2, and BH3) of Mcl-1 are required for interaction with tBid. tBID BCL2 apoptosis regulator Homo sapiens