This gene encodes a protein that is 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 and a large and 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 caspase is able to cleave and activate its own precursor protein, as well as caspase 1 precursor. When overexpressed, this gene induces cell apoptosis. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008].
Dernières publications pour nos Caspase 4 Protéines
Xia, Yang, Bu, Ji, Zhao, Zheng, Lin, Li, Lu: "Differential regulation of c-Jun protein plays an instrumental role in chemoresistance of cancer cells." dans: The Journal of biological chemistry, Vol. 288, Issue 27, pp. 19321-9, (2013) (PubMed).
Murakami, Tolstykh, Bao, Niu, Steuer, Bao, Chang, Espiritu, Bansal, Lam, Otto, Sofia, Furman: "Mechanism of activation of PSI-7851 and its diastereoisomer PSI-7977." dans: The Journal of biological chemistry, Vol. 285, Issue 45, pp. 34337-47, (2010) (PubMed).
Chen, Xia, Fang, Hawke, Lu: "Caspase-10-mediated heat shock protein 90 beta cleavage promotes UVB irradiation-induced cell apoptosis." dans: Molecular and cellular biology, Vol. 29, Issue 13, pp. 3657-64, (2009) (PubMed).
Hasegawa, Yamada, Komiyama, Hayashi, Ishibashi, Sunazuka, Izuhara, Sugahara, Tsuruda, Masuda, Takasu, Tsukasaki, Tomonaga, Kamihira et al.: "A novel natural compound, a cycloanthranilylproline derivative (Fuligocandin B), sensitizes leukemia cells to apoptosis induced by tumor necrosis factor related apoptosis-inducing ligand (TRAIL) ..." dans: Blood, Vol. 110, Issue 5, pp. 1664-74, (2007) (PubMed).