Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3.
We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg(+2), Mn(+2), Zn(2+), and Co(2+)) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe(+2) and Ca(+2) do not function as MST3 cofactors. Mn(2+), Co(2+), and Mg(2+)-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn(2+)-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn(2+) as the metal ion cofactor of a recombinant serine/threonine kinase.
Lu
Te-Jung
TJ
Department of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan.
Huang
Chi-Ying F
CY
Yuan
Chiun-Jye
CJ
Lee
Yuan-Chii
YC
Leu
Tzeng-Horng
TH
Chang
Wen-Chang
WC
Lu
Te-Ling
TL
Jeng
Wen-Yih
WY
Lai
Ming-Derg
MD
D000818:Animals; D019556:COS Cells; D002413:Cations, Divalent / Q000378:metabolism / Q000494:pharmacology; D002522:Chlorocebus aethiops; D003035:Cobalt / Q000378:metabolism; D003067:Coenzymes / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D066298:In Vitro Techniques; D007700:Kinetics; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
D002413:Cations, Divalent; D003067:Coenzymes; D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D003035:Cobalt; D004492:Edetic Acid; D017346:Protein Serine-Threonine Kinases; D015032:Zinc