14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves

scientific article published on 01 July 1999

14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/S0014-5793(99)00868-6
P8608Fatcat IDrelease_icdn2xbrxbaojdtcln525xb5ee
P698PubMed publication ID10428475

P2093author name stringH Weiner
W M Kaiser
P2860cites workThe inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 proteinQ71171758
Plant metabolism: enzyme regulation by 14-3-3 proteinsQ71824288
Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletionQ72310731
Antibodies That Distinguish between the Serine-158 Phospho- and Dephospho-Form of Spinach Leaf Sucrose-Phosphate SynthaseQ74781499
Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteinsQ77790311
Short-term effects of nitrate on sucrose synthesis in wheat leavesQ86638539
Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserineQ24322674
Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathwaysQ27729753
A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activityQ28276506
Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteinsQ28293607
The structural basis for 14-3-3:phosphopeptide binding specificityQ29547190
Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylationQ29614709
14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteinsQ35624026
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitorsQ36237082
A conserved acidic motif in the N-terminal domain of nitrate reductase is necessary for the inactivation of the enzyme in the dark by phosphorylation and 14-3-3 bindingQ38329724
Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin.Q38353528
14-3-3 proteins: structure resolved, functions less clearQ40427588
Nitrate: nutrient and signal for plant growthQ40462834
Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteinsQ44870214
Regulation of sucrose-phosphate-synthase activity in spinach leaves by protein level and covalent modificationQ44870508
Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways.Q48667801
Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylationQ68156237
P433issue1-2
P921main subjectproteolysisQ33123
P304page(s)75-78
P577publication date1999-07-01
P1433published inFEBS LettersQ1388051
P1476title14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves
P478volume455

Reverse relations

cites work (P2860)
Q3440554014-3-3 proteins; bringing new definitions to scaffolding
Q8643461714-3-3 regulates 1-aminocyclopropane-1-carboxylate synthase protein turnover in Arabidopsis
Q3088009514-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells
Q45153587A Robot-based platform to measure multiple enzyme activities in Arabidopsis using a set of cycling assays: comparison of changes of enzyme activities and transcript levels during diurnal cycles and in prolonged darkness
Q42114522A model for the circadian oscillations in expression and activity of nitrate reductase in higher plants.
Q35176852Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1.
Q51949807Beta-subunits of the SnRK1 complexes share a common ancestral function together with expression and function specificities; physical interaction with nitrate reductase specifically occurs via AKINbeta1-subunit.
Q73084597Binding to 14-3-3 proteins is not sufficient to inhibit nitrate reductase in spinach leaves
Q34667579Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity.
Q44764590Control of nitrate reductase by circadian and diurnal rhythms in tomato
Q73907275Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties
Q64240990Extensive Variations in Diurnal Growth Patterns and Metabolism Among spp. Strains
Q73591709Increased glutamine synthetase activity and changes in amino acid pools in leaves treated with 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR)
Q30475806Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions.
Q35040499Metabolic enzymes as targets for 14-3-3 proteins
Q52584644Nitrate Reductases Are Relocalized to the Nucleus by AtSIZ1 and Their Levels Are Negatively Regulated by COP1 and Ammonium.
Q38078367Nitric oxide in plants: an assessment of the current state of knowledge.
Q46681874Phosphorylation and subsequent interaction with 14-3-3 proteins regulate plastid glutamine synthetase in Medicago truncatula
Q34053551Regulatory 14-3-3 protein-protein interactions in plant cells
Q37425274Ribosome and transcript copy numbers, polysome occupancy and enzyme dynamics in Arabidopsis.
Q36241760Role of 14-3-3 proteins in eukaryotic signaling and development
Q34667530Sugar sensing and signaling in plants
Q35166332The 14-3-3 proteins: gene, gene expression, and function
Q39250062p70S6K1 (S6K1)-mediated Phosphorylation Regulates Phosphatidylinositol 4-Phosphate 5-Kinase Type I γ Degradation and Cell Invasion.

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