[HTML][HTML] Both phosphorylation and caspase-mediated cleavage contribute to regulation of the Ste20-like protein kinase Mst1 during CD95/Fas-induced apoptosis
JD Graves, KE Draves, Y Gotoh, EG Krebs… - Journal of Biological …, 2001 - ASBMB
The serine/threonine kinase Mst1, a mammalian homolog of the budding yeast Ste20
kinase, is cleaved by caspase-mediated proteolysis in response to apoptotic stimuli such as
ligation of CD95/Fas or treatment with staurosporine. Furthermore, overexpression of Mst1
induces morphological changes characteristic of apoptosis in human B lymphoma cells.
Mst1 may therefore represent an important target for caspases during cell death which
serves to amplify the apoptotic response. Here we report that Mst1 has two caspase …
kinase, is cleaved by caspase-mediated proteolysis in response to apoptotic stimuli such as
ligation of CD95/Fas or treatment with staurosporine. Furthermore, overexpression of Mst1
induces morphological changes characteristic of apoptosis in human B lymphoma cells.
Mst1 may therefore represent an important target for caspases during cell death which
serves to amplify the apoptotic response. Here we report that Mst1 has two caspase …
