caspase-6; MCH-2 protein (CASP6, MCH2)
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Function
- role in the activation cascade of caspases responsible for apoptosis execution
- cleaves poly(ADP-ribose) polymerase & lamins in vitro
- cleaves DNA topoisomerase 1
- may participate in processing of amyloid precursor protein (APP)[2]
- overexpression promotes programmed cell death
- activation is suppressed by phosphorylation at Ser-257
- cleavages by caspase-3, caspase-8 or caspase-10 generate the two active subunits
- strict requirement for Asp at position P1 & has a preferred cleavage sequence of Val-Glu-His-Asp-|-
Structure
- heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kD (p18) & a 11 kD (p11) subunit
- belongs to the peptidase C14 family
Compartment
Alternative splicing
named isoforms=2
More general terms
More specific terms
References
- ↑ Martin SJ, Green DR. Protease activation during apoptosis: death by a thousand cuts? Cell. 1995 Aug 11;82(3):349-52. Review. No abstract available. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7634323
- ↑ 2.0 2.1 Rampon C, Jiang CH, Dong H, Tang YP, Lockhart DJ, Schultz PG, Tsien JZ, Hu Y. Effects of environmental enrichment on gene expression in the brain. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12880-4. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11070096
- ↑ UniProt http://www.uniprot.org/uniprot/P55212.html