• Interaction

    AccNo. 54284 Score 0.49
    Name PM_8940132
    Kd 1.0

    Peptide

    AccNo. 54162
    Name YVAD
    Sequence YVAD
    54162_small
    Internalized no
    Is Motif no

    Interactor

    AccNo. 53784
    Name unknown

    Experiment

    AccNo. 54125
    Classification incorrect?
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    Voting_motivation
    CA CVD DM APO ANG MI BD
    0.88 0.49 0.42 0.99 0.61 0.14 0.32 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PM_8940132
    Detection unspecified method, MI:0686
    Source Pubmed Text Id 8940132
    Journal J Biol Chem. 1996 Dec 6;271(49):31277-82.
    Title Specific cleavage of alpha-fodrin during Fas- and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1beta-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease.
    Authors Cryns VL, Bergeron L, Zhu H, Li H, Yuan J
    Text Interleukin-1beta-converting enzyme (ICE)/Ced-3 proteases play a critical role in apoptosis. One well characterized substrate of these proteases is the DNA repair enzyme poly(ADP-ribose) polymerase. We report here that alpha-fodrin, an abundant membrane-associated cytoskeletal protein, is cleaved rapidly and specifically during Fas- and tumor necrosis factor-induced apoptosis; this cleavage is mediated by an ICE/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease. Studies in cells treated with these apoptotic stimuli reveal that both fodrin and poly(ADP-ribose) polymerase proteolysis are inhibited by acetyl-Tyr-Val-Ala-Asp chloromethyl ketone and CrmA, specific inhibitors of ICE/Ced-3 proteases. However, fodrin proteolysis can be distinguished from poly(ADP-ribose) polymerase proteolysis by its relative insensitivity to acetyl-Asp-Glu-Val-Asp aldehyde (DEVD-CHO), a selective inhibitor of a subset of ICE/Ced-3 proteases that includes CPP32. DEVD-CHO protects cells from Fas-induced apoptosis but does not prevent fodrin proteolysis, indicating that cleavage of this protein can be uncoupled from apoptotic cell death. Moreover, purified fodrin is cleaved in vitro by CPP32 (but not by ICE) into fragments of the same size observed in vivo during apoptosis. These findings suggest that fodrin proteolysis in vivo may reflect the activity of multiple ICE/Ced-3 proteases whose partial sensitivity to DEVD-CHO reflects a limited contribution from CPP32, or an ICE/Ced-3 protease less sensitive than CPP32 to DEVD-CHO inhibition.
    Mesh Terms Antigens, CD95/pharmacology; Apoptosis; Caenorhabditis elegans Proteins; Carrier Proteins/metabolism; Caspase 1; Caspases; Cysteine Endopeptidases/metabolism; Cysteine Proteinase Inhibitors/pharmacology; Glycoproteins/pharmacology; Hela Cells; Helminth Proteins/metabolism; Humans; Jurkat Cells; Microfilament Proteins/metabolism; Oligopeptides/metabolism; Spectrin/metabolism; Tumor Necrosis Factor-alpha/pharmacology
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