Phosphorylation of STK3 (MST2) and SAV1 by STK3

Stable Identifier
Reaction [transition]
Homo sapiens
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The serine/threonine kinase STK3 (MST2) catalyzes its own autophosphorylation as well as the phosphorylation of SAV1. These two reactions are annotated here as a single concerted process that takes place in a tetrameric complex containing two STK3 (MST2) subunits and two SAV1 subunits, based on the observations that STK3 (MST2) can catalyze both phosphorylation reactions in vitro, as well as the observations that each protein dimerizes and that STK3 (MST2) and SAV1 associate to form a complex. The order in which the various components associate, the stoichiometry of the complex ultimately formed, and the point(s) in this association process at which phosphoryltion occurs have not been established in vitro or in vivo, however (Callus et al. 2006; Praskova et al. 2004).
Literature References
PubMed ID Title Journal Year
15109305 Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras

Ortiz-Vega, S, Khoklatchev, A, Praskova, M, Avruch, J

Biochem J 2004
15688006 The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1

Chalamalasetty, RB, Nigg, EA, Nousiainen, M, Chan, EH, Silljé, HH, Schäfer, A

Oncogene 2005
16930133 Association of mammalian sterile twenty kinases, Mst1 and Mst2, with hSalvador via C-terminal coiled-coil domains, leads to its stabilization and phosphorylation

Callus, BA, Vaux, DL, Verhagen, AM

FEBS J 2006
Catalyst Activity

protein serine/threonine kinase activity of STK3:SAV1 [cytosol]

Orthologous Events
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