Caspase-15 is autoprocessed at two sites that contain an aspartate residue in the P1′ position

Biochemical and Biophysical Research Communications

Volumn 350, Issue 4, 2006, Pages 955-959

  Eckhart, Leopold ^a   Kittel, Christian ^a   Ballaun, Claudia ^a   Tschachler, Erwin ^a,b  

^a Universitatsklinik fur Dermatologie   (Austria)

^b Centre de Recherches et d'Investigations Epidermiques et Sensorielles CERIES   (France)

Author keywords

Apoptosis; Autoprocessing; Caspase; Enzyme activation; P1 residue; Specificity of cleavage

Indexed keywords

ASPARTIC ACID; CASPASE 15; ENZYME; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CLADISTICS; EMBRYO; HUMAN; HUMAN CELL; MAMMAL; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; ASPARTIC ACID; BINDING SITES; CASPASES; CONSERVED SEQUENCE; ENZYME ACTIVATION; EVOLUTION, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID;

LAURASIATHERIA; MAMMALIA; SUIDAE;

EID: 33750036392     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.130     Document Type: Article

References (23)

1. Degterev A., Boyce M., and Yuan J. A decade of caspases. Oncogene 22 (2003) 8543-8567
2. Koenig U., Eckhart L., and Tschachler E. Evidence that caspase-13 is not a human but a bovine gene. Biochem. Biophys. Res. Commun. 285 (2001) 1150-1154
3. Lamkanfi M., Declercq W., Kalai M., Saelens X., and Vandenabeele P. Alice in caspase land. A phylogenetic analysis of caspases from worm to man. Cell Death Differ. 9 (2002) 358-361
4. Eckhart L., Ballaun C., Uthman A., Kittel C., Stichenwirth M., Buchberger M., Fischer H., Sipos W., and Tschachler E. Identification and characterization of a novel mammalian caspase with proapoptotic activity. J. Biol. Chem. 280 (2005) 35077-35080
5. Chang D.W., Ditsworth D., Liu H., Srinivasula S.M., Alnemri E.S., and Yang X. Oligomerization is a general mechanism for the activation of apoptosis initiator and inflammatory procaspases. J. Biol. Chem. 278 (2003) 16466-16469
6. Riedl S.J., and Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5 (2004) 897-907
7. Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
8. Stennicke H.R., Deveraux Q.L., Humke E.W., Reed J.C., Dixit V.M., and Salvesen G.S. Caspase-9 can be activated without proteolytic processing. J. Biol. Chem. 274 (1999) 8359-8362
9. Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T., Garcia-Calvo M., Houtzager V.M., Nordstrom P.A., Roy S., Vaillancourt J.P., Chapman K.T., and Nicholson D.W. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272 (1997) 17907-17911
10. Eckhart L., Uthman A., Sipos W., and Tschachler E. Genome sequence comparison reveals independent inactivation of the caspase-15 gene in different evolutionary lineages of mammals. Mol. Biol. Evol. 23 (2006) 2081-2089
11. Talanian R.V., Quinlan C., Trautz S., Hackett M.C., Mankovich J.A., Banach D., Ghayur T., Brady K.D., and Wong W.W. Substrate specificities of caspase family proteases. J. Biol. Chem. 272 (1997) 9677-9682
12. Stennicke H.R., Renatus M., Meldal M., and Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350 (2000) 563-568
13. Petrassi H.M., Williams J.A., Li J., Tumanut C., Ek J., Nakai T., Masick B., Backes B.J., and Harris J.L. A strategy to profile prime and non-prime proteolytic substrate specificity. Bioorg. Med. Chem. Lett. 15 (2005) 3162-3166
14. Prasad S., Soldatenkov V.A., Srinivasarao G., and Dritschilo A. Identification of keratins 18, 19 and heat-shock protein 90 beta as candidate substrates of proteolysis during ionizing radiation-induced apoptosis of estrogen-receptor negative breast tumor cells. Int. J. Oncol. 13 (1998) 757-764
15. Eckhart L., Declercq W., Ban J., Rendl M., Lengauer B., Mayer C., Lippens S., Vandenabeele P., and Tschachler E. Terminal differentiation of human keratinocytes and stratum corneum formation is associated with caspase-14 activation. J. Invest. Dermatol. 115 (2000) 1148-1151
16. Springer M.S., Murphy W.J., Eizirik E., and O'Brien S.J. Placental mammal diversification and the Cretaceous-Tertiary boundary. Proc. Natl. Acad. Sci. USA 100 (2003) 1056-1061
17. Denault J.B., Bekes M., Scott F.L., Sexton K.M., Bogyo M., and Salvesen G.S. Engineered hybrid dimers: tracking the activation pathway of caspase-7. Mol. Cell 23 (2006) 523-533
18. Yamin T.T., Ayala J.M., and Miller D.K. Activation of the native 45-kDa precursor form of interleukin-1-converting enzyme. J. Biol. Chem. 271 (1996) 13273-13282
19. Li H., Bergeron L., Cryns V., Pasternack M.S., Zhu H., Shi L., Greenberg A., and Yuan J. Activation of caspase-2 in apoptosis. J. Biol. Chem. 272 (1997) 21010-21017
20. Medema J.P., Scaffidi C., Kischkel F.C., Shevchenko A., Mann M., Krammer P.H., and Peter M.E. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J. 16 (1997) 2794-2804
21. Liu H., Chang D.W., and Yang X. Interdimer processing and linearity of procaspase-3 activation. A unifying mechanism for the activation of initiator and effector caspases. J. Biol. Chem. 280 (2005) 11578-11582
22. Yan N., and Shi Y. Mechanisms of apoptosis through structural biology. Annu. Rev. Cell. Dev. Biol. 21 (2005) 35-56
23. E.H. Margulies, J.P. Vinson, NISC Comparative Sequencing Program, W. Miller, D.B. Jaffe, K. Lindblad-Toh, J.L. Chang, E.D. Green, E.S. Lander, J.C. Mullikin, M. Clamp, An initial strategy for the systematic identification of functional elements in the human genome by low-redundancy comparative sequencing. Proc. Natl. Acad. Sci. USA 102 (2005) 4795-4800.