Entry |
|
Name |
caspase-6;
CASP-6;
apoptotic protease Mch-2;
Mch2
|
Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
|
Reaction(IUBMB) |
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp!
|
Comment |
Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60) [2]. These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype [2]. Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to the release of cytochrome c from the mitochondria. The release of cytochrome c is an essential component of the intrinsic apoptosis pathway [1]. The enzyme can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragmentation in the final phases of apoptosis [2,4,5,6]. Belongs in peptidase family C14.
|
History |
EC 3.4.22.59 created 2007
|
Orthology |
|
Genes |
» show all
|
Reference |
|
Authors |
Cowling V, Downward J. |
Title |
Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain. |
Journal |
|
Reference |
|
Authors |
Chang HY, Yang X. |
Title |
Proteases for cell suicide: functions and regulation of caspases. |
Journal |
|
Reference |
|
Authors |
Kang BH, Ko E, Kwon OK, Choi KY. |
Title |
The structure of procaspase 6 is similar to that of active mature caspase 6. |
Journal |
|
Reference |
|
Authors |
Lee SC, Chan J, Clement MV, Pervaiz S. |
Title |
Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop. |
Journal |
|
Reference |
|
Authors |
MacLachlan TK, El-Deiry WS. |
Title |
Apoptotic threshold is lowered by p53 transactivation of caspase-6. |
Journal |
|
Reference |
|
Authors |
Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, Moir RD, Goldman RD, Poirier GG, Kaufmann SH, Earnshaw WC. |
Title |
Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. |
Journal |
|
Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.22.59 |
|