Caspase 8

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Caspase 8, apoptosis-related cysteine peptidase
PDB rendering based on 1f9e.
Available structures
1f9e, 1i4e, 1qdu, 1qtn, 2c2z, 2fun
Identifiers
Symbols	CASP8; CAP4; FLICE; MACH; MCH5; MGC78473
External IDs	OMIM: 601763 MGI: 1261423 HomoloGene: 7657
Gene ontology Molecular function • signal transducer activity • protein binding • cysteine-type peptidase activity • caspase activity • identical protein binding Cellular component • nucleus • cytoplasm • mitochondrion • cytoskeleton • Noc1p-Noc2p complex Biological process • angiogenesis • neural tube formation • proteolysis • heart development • apoptotic program • macrophage differentiation • regulation of apoptosis • positive regulation of I-kappaB kinase/NF-kappaB cascade
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	841	12370
Ensembl	ENSG00000064012	ENSMUSG00000026029
UniProt	Q14790	Q3U607
RefSeq	NM_001080124 (mRNA)	NM_001080126 (mRNA)
	NP_001073593 (protein)	NP_001073595 (protein)
Location	Chr 2: 201.81 - 201.86 Mb	Chr 1: 58.74 - 58.79 Mb
PubMed search	[1]	[2]

Caspase 8 is a caspase protein. It most likely acts upon caspase 3.

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.^[1]

Signaling pathway of TNF-R1. Dashed grey lines represent multiple steps

Interactions

Caspase 8 has been shown to interact with CFLAR,^{[2][3][4][5][6][7][8]} PEA15,^[9][10] Caspase 10,^{[11][2][12][13]} Caspase-9,^[12][13] Fas receptor,^[11][3][14] Fas ligand,^[11][2] Caspase 7,^[12][13] NOL3,^[15] BH3 interacting domain death agonist,^[11][12] DEDD,^[16][17][18] TRAF1,^[2][19] Bcl-2,^[20][12] RIPK1,^[21][22][23] TNFRSF10B,^[11][14] FADD,^{[11][2][5][24][25][22][26]} BCAP31,^[27] IFT57,^[28] Caspase 3,^[12][13] Caspase 2^[12][13] and Caspase 6.^[29][12][13]

Overview of signal transduction pathways involved in apoptosis.

References

Further reading

v • d • e PDB Gallery 1f9e: CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO   1i4e: CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX   1qdu: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK   1qtn: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE   2c2z: CRYSTAL STRUCTURE OF CASPASE-8 IN COMPLEX WITH AZA-PEPTIDE MICHAEL ACCEPTOR INHIBITOR   2fun: alternative p35-caspase-8 complex

See also

• The Proteolysis Map
• FADD

External links

• Apoptosis & Caspase 8 - The Proteolysis Map-animation
• MeSH Caspase+8