EC 3.4.22.63 - Caspase-10

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.22.63

Names

Accepted name:
caspase-10
Other names:
FLICE2
Mch4
CASP-10
ICE-like apoptotic protease 4
apoptotic protease Mch-4
FAS-associated death domain protein interleukin-1β-converting enzyme 2
Systematic name:
-

Reaction

Comments:

Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62) [1]. Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation [1]. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-κB survival signalling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation) [2]. Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp┼ to yield the pro-apoptotic p15 fragment. The p15 fragment is N-myristoylated and enhances cytochrome c release from mitochondria (which initiatiates the intrinsic apoptosis pathway). Bid can be further cleaved by caspase-10 and granzyme B but not by caspase-3 and caspase-8 at Ile-Glu-Thr-Asp┼ to yield a p13 fragment that is not N-myristoylated [2]. Belongs in peptidase family C14.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00864
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Chang, H.Y. and Yang, X.
    Proteases for cell suicide: functions and regulation of caspases.
    Microbiol. Mol. Biol. Rev. 64: 821-846 (2000). [PMID: 11104820]
  2. Fischer, U., Stroh, C. and Schulze-Osthoff, K.
    Unique and overlapping substrate specificities of caspase-8 and caspase-10.
    Oncogene 25: 152-159 (2006). [PMID: 16186808]
  3. Shikama, Y., Yamada, M. and Miyashita, T.
    Caspase-8 and caspase-10 activate NF-κB through RIP, NIK and IKKα kinases.
    Eur. J. Immunol. 33: 1998-2006 (2003). [PMID: 12884866]
  4. Boatright, K.M., Deis, C., Denault, J.-B., Sutherlin, D.P. and Salvesen, G.S.
    Activation of caspases-8 and -10 by FLIPL.
    Biochem. J. 382: 651-657 (2004). [PMID: 15209560]

[EC 3.4.22.63 created 2007]