[HTML][HTML] Mapping of MST1 kinase sites of phosphorylation: activation and autophosphorylation
H Glantschnig, GA Rodan, AA Reszka - Journal of Biological Chemistry, 2002 - ASBMB
MST1 is a member of the Sterile-20 family of cytoskeletal, stress, and apoptotic kinases.
MST1 is activated by phosphorylation at previously unidentified sites. This study examines
the role of phosphorylation at several sites and effects on kinase activation. We define Thr
183 in subdomain VIII as a primary site of phosphoactivation. Thr 187 is also critical for
kinase activity. Phosphorylation of MST1 in subdomain VIII was catalyzed by active MST1
via intermolecular autophosphorylation, enhanced by homodimerization. Active MST1 (wild …
MST1 is activated by phosphorylation at previously unidentified sites. This study examines
the role of phosphorylation at several sites and effects on kinase activation. We define Thr
183 in subdomain VIII as a primary site of phosphoactivation. Thr 187 is also critical for
kinase activity. Phosphorylation of MST1 in subdomain VIII was catalyzed by active MST1
via intermolecular autophosphorylation, enhanced by homodimerization. Active MST1 (wild …