Activation of an S6 Kinase From Human Placenta by Autophosphorylation

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Article describing a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. The data supports the hypothesis that this previously uncharacterized S6 kinase belongs to a unique family of protein kinases which utilize autophosphorylation as part of their in vivo activation mechanism.

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9 p.

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Dennis, Patrick B. & Masaracchia, Ruthann A. September 15, 1993.

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Article describing a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. The data supports the hypothesis that this previously uncharacterized S6 kinase belongs to a unique family of protein kinases which utilize autophosphorylation as part of their in vivo activation mechanism.

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9 p.

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This research was originally published in the Journal of Biological Chemistry. Dennis & Masaracchia. Activation of an S6 kinase from human placenta by autophosphorylation. J. Biol. Chem. 1993; 268:19833-19841. © the American Society for Biochemistry and Molecular Biology.

Abstract: A number of protein kinases have been shown to undergo autophosphorylation, but few have demonstrated a coordinate increase or decrease in enzymatic activity as a result. Described here is a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. This S6/H4 kinase, purified in an inactive state, exhibited a molecular mass of 60 kDa as estimated by SDS-polyacrylamide gel electrophoresis. The 60-kDa protein underwent autophosphorylation, was labeled by 8-azido-[alpha-32P]ATP, and reacted with an antibody to the conserved APE domain of the cAMP-dependent protein kinase. The protein did not cochromatograph with p70 S6 kinase and did not cross-react with an anti-p70 kinase antibody. The synthetic peptide S6-21, histone H4, and myelin basic protein were phosphorylated by the purified S6/H4 kinase. Mild digestion of the inactive S6/H4 kinase with trypsin generated a 40-kDa fragment, as determined by SDS-polyacrylamide gel electrophoresis. The trypsin treatment was necessary, but not sufficient, to fully activate the kinase. Subsequent incubation of the trypsin-treated S6 kinase with MgATP resulted in the rapid autophosphorylation of the 40-kDa fragment along with a coordinate increase in kinase activity. The autophosphorylation of the 40-kDa protein was positively correlated with MgATP incubation time and an increase in activity toward the S6-21 peptide, histone H4, and myelin basic protein. Taken together, these data support the hypothesis that this previously uncharacterized S6 kinase belongs to a unique family of protein kinases which utilize autophosphorylation as part of their in vivo activation mechanism.

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  • Journal of Biological Chemistry, 268(26), American Society for Biochemistry and Molecular Biology, September 15 1993, pp. 19833-19841

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  • Publication Title: Journal of Biological Chemistry
  • Volume: 268
  • Issue: 26
  • Page Start: 19833
  • Page End: 19841
  • Pages: 9
  • Peer Reviewed: Yes

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  • September 15, 1993

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  • Dec. 17, 2021, 8:13 p.m.

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  • Jan. 13, 2022, 11:26 a.m.

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Dennis, Patrick B. & Masaracchia, Ruthann A. Activation of an S6 Kinase From Human Placenta by Autophosphorylation, article, September 15, 1993; [Rockville, Maryland]. (https://digital.library.unt.edu/ark:/67531/metadc1871047/: accessed March 22, 2023), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT College of Science.

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