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 undergoes a robust autoactivation in vitro, mediated by an intramolecular autophosphorylation on the activation loop of an MST dimer. 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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Biochemical Society transactions, 32(Pt3), 485-488 (2004-05-26)
Mammalian Sterile20-like kinase 1 (Mst1) is a ubiquitously expressed serine/threonine kinase which represents a member of the rapidly expanding family of enzymes related to the yeast Sterile20 kinase. Although the physiological function of Mst1 and its role in intracellular signalling
The six human Nore1/RASSF genes encode a family of putative tumor suppressor proteins, each expressed as multiple mRNA splice variants. The predominant isoforms of these noncatalytic polypeptides are characterized by the presence in their carboxyterminal segments of a Ras-Association (RA)
The Hippo tumor suppressor pathway is essential for development and tissue growth control, encompassing a core cassette consisting of the Hippo (MST1/2), Warts (LATS1/2), and Tricornered (NDR1/2) kinases together with MOB1 as an important signaling adaptor. However, it remains unclear
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