Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
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منابع مشابه
Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
BACKGROUND Nitrate reductase (NR) in leaves is rapidly inactivated in the dark by a two-step mechanism in which phosphorylation of NR on the serine at position 543 (Ser543) promotes binding to nitrate reductase inhibitor protein (NIP). The eukaryotic 14-3-3 proteins bind to many mammalian signalling components (Raf-1, Bcr, phosphoinositide 3-kinase, protein kinase C, polyomavirus middle-T antig...
متن کاملPhosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an amp-binding site on 14-3-3 proteins.
The inactivation of phosphorylated nitrate reductase (NR) by the binding of 14-3-3 proteins is one of a very few unambiguous biological functions for 14-3-3 proteins. We report here that serine and threonine residues at the +6 to +8 positions, relative to the known regulatory binding site involving serine-543, are important in the interaction with GF14omega, a recombinant plant 14-3-3. Also sho...
متن کاملDivalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase.
Binding of 14-3-3 proteins to nitrate reductase phosphorylated on Ser543 (phospho-NR) inhibits activity and is responsible for the inactivation of nitrate reduction that occurs in darkened leaves. The 14-3-3-dependent inactivation of phospho-NR is known to require millimolar concentrations of a divalent cation such as Mg2+ at pH 7.5. We now report that micromolar concentrations of the polyamine...
متن کاملFusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins.
Plants acquire potassium (K+) ions for cell growth and movement via regulated diffusion through K+ channels. Here, we present crystallographic and functional data showing that the K+ inward rectifier KAT1 (K+Arabidopsis thaliana 1) channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H+-ATPase. We identified a 14-3-3 mode III binding site...
متن کامل14-3-3 Regulates Actin Dynamics by Stabilizing Phosphorylated Cofilin
The functionality of the actin cytoskeleton depends on a dynamic equilibrium between filamentous and monomeric actin. Proteins of the ADF/cofilin family are essential for the high rates of actin filament turnover observed in motile cells through regulation of actin polymerization/depolymerization cycles. Rho GTPases act through p21-activated kinase-1 (Pak-1) and Rho kinase to inhibit cofilin ac...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1996
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(02)70677-5