Caspase

Caspase (CASP) are cysteine-aspartic proteases (see Protease) which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP.

CASP-1 (or Interleukin-1 beta converting enzyme, ICE) cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. See:

Human Caspase-1

CASP-3 or (Apopain; Cysteine protease CPP32) interacts with CASP-8 and CASP-9 during cell apoptosis. See:

Sandox Bay Serrano

Student Projects for UMass Chemistry 423 Spring 2012-5
Caspase-3 Regulatory Mechanisms

CASP-4 binds the lipid moiety of lipopolysaccharide to induce the activation of non-canonical inflammasome^[1].
CASP-6 is involved in the activation of cascade of caspases during apoptosis. See:

Molecular Playground/Caspase-6 (new)

Caspase-6 and neurodegeneration

CASP-7 is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits. CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in Drosophila melanogaster. See:

Molecular Playground/Caspase-7 Dynamics

Molecular Playground/Executioner Caspase-7

CASP-9 is an aspartic protease linked to mitochondrial death pathway. See:

Molecular Playground/Caspase-9 Regulation.

Metacaspase (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi.

^[2]^[3]

3D structures of caspase

Caspase 3D structures

CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, 1pyo

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Lagrange B, Benaoudia S, Wallet P, Magnotti F, Provost A, Michal F, Martin A, Di Lorenzo F, Py BF, Molinaro A, Henry T. Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11. Nat Commun. 2018 Jan 16;9(1):242. doi: 10.1038/s41467-017-02682-y. PMID:29339744 doi:http://dx.doi.org/10.1038/s41467-017-02682-y
↑ Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:http://dx.doi.org/10.1074/jbc.M304895200
↑ Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:http://dx.doi.org/10.1038/370270a0

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Michal Harel, Alexander Berchansky

[1] Lagrange B, Benaoudia S, Wallet P, Magnotti F, Provost A, Michal F, Martin A, Di Lorenzo F, Py BF, Molinaro A, Henry T. Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11. Nat Commun. 2018 Jan 16;9(1):242. doi: 10.1038/s41467-017-02682-y. PMID:29339744 doi:http://dx.doi.org/10.1038/s41467-017-02682-y

[2] Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:http://dx.doi.org/10.1074/jbc.M304895200

[3] Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:http://dx.doi.org/10.1038/370270a0

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Caspase

3D structures of caspase

ReferencesReferences

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