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Overview
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MST1 belongs to a family of proteins that share similarity with a budding yeast serine/threonine kinase, sterile-20 (Ste20). Endogenous full-length MST1 is activated by a variety of stressful stimuli, accompanied by the secondary appearance of a 36 kDa Thr183-phosphorylated, caspase-cleaved catalytic fragment. Recombinant MST1 undergo a robust autoactivation in vitro, mediated by an intramolecular autophosphorylation on the activation loop of an MST dimmer. MST1 can initiate apoptosis when transiently overexpressed in mammalian cells. Interference with the ability of endogenous MST1 to associate with the putative tumor suppressor proteins Nore1/RASSF can inhibit Ras-induced apoptosis.
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