Post-translational regulation of nitrate reductase activity: A role for Ca2+ and 14-3-3 proteins

Steven C. Huber, Markus Bachmann, Joan L. Huber

Research output: Contribution to journalReview article

Abstract

The control of nitrate reductase (NR) activity by reversible protein phosphorylation is a two-stage process: the enzyme is reversibly phosphorylated, and the phosphorylated form then binds an inhibitor protein. Recent results indicate that the phosphorylation reaction is Ca2+-dependent and that the inhibitor is a member of the 14-3-3 family of proteins. These results suggest the convergence of several signal transduction pathways in the control of nitrate assimilation. Recent results also implicate metabolites and 5'-AMP as possible effectors regulating the phosphorylation status of NR in vivo.

Original languageEnglish (US)
Pages (from-to)432-438
Number of pages7
JournalTrends in Plant Science
Volume1
Issue number12
DOIs
StatePublished - Dec 1996

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nitrate reductase
phosphorylation
calcium
protein phosphorylation
signal transduction
assimilation (physiology)
proteins
nitrates
metabolites
enzymes

ASJC Scopus subject areas

  • Plant Science

Cite this

Post-translational regulation of nitrate reductase activity : A role for Ca2+ and 14-3-3 proteins. / Huber, Steven C.; Bachmann, Markus; Huber, Joan L.

In: Trends in Plant Science, Vol. 1, No. 12, 12.1996, p. 432-438.

Research output: Contribution to journalReview article

Huber, Steven C. ; Bachmann, Markus ; Huber, Joan L. / Post-translational regulation of nitrate reductase activity : A role for Ca2+ and 14-3-3 proteins. In: Trends in Plant Science. 1996 ; Vol. 1, No. 12. pp. 432-438.
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