Caspase-mediated cleavage of MST3

Stable Identifier
Reaction [transition]
Homo sapiens
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Caspase-mediated cleavage of Mst3 activates its intrinsic kinase activity. Proteolytic removal of the COOH-terminal domain promotes nuclear translocation of its kinase domain. Ectopic expression of COOH-terminal truncated Mst3 results in DNA fragmentation and morphological changes characteristic of apoptosis (Huang et al., 2002). Both CASP3 and CASP7 can cleave MST3, and phosphorylation of MST3 may promote facilitate caspase-mediated cleavage (Turowec et al. 2014).

Literature References
PubMed ID Title Journal Year
12107159 Caspase activation of mammalian sterile 20-like kinase 3 (Mst3). Nuclear translocation and induction of apoptosis

Huang, CY, Hsu, CY, Fang, HI, Robinson, DR, Wu, YM, Huang, CL, Lai, MD, Yuan, CJ, Kung, HJ, Leu, TH, Shih, HM, Lee, WS, Lu, TJ

J Biol Chem 2002
24556848 An unbiased proteomic screen reveals caspase cleavage is positively and negatively regulated by substrate phosphorylation

Graves, LM, Johnson, GL, Knight, JD, Lajoie, GA, Litchfield, DW, Li, SS, Turowec, JP, Smalley, DM, Zukowski, SA

Mol. Cell Proteomics 2014
Catalyst Activity

cysteine-type endopeptidase activity of Caspase-3, Caspase-7 [cytosol]

Orthologous Events
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