Regulation of cytosolic enzymes in primary metabolism by reversible protein phosphorylation

Current Opinion in Plant Biology

Volumn 1, Issue 3, 1998, Pages 224-229

  MacKintosh, Carol ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; MESSENGER RNA; PROTEIN; PROTEIN 14 3 3; TYROSINE 3 MONOOXYGENASE; VEGETABLE PROTEIN;

CYTOSOL; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING; REVIEW; SIGNAL TRANSDUCTION;

14-3-3 PROTEINS; CYTOSOL; ENZYME ACTIVATION; ENZYMES; PHOSPHORYLATION; PLANT PROTEINS; PROTEIN BINDING; PROTEINS; RNA, MESSENGER; SIGNAL TRANSDUCTION; TYROSINE 3-MONOOXYGENASE;

EID: 0032082523     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(98)80108-8     Document Type: Article

References (8)

1. Scheible W-R, Lauerer M, Schulze E-D, Caboche M, Stitt M: Accumulation of nitrate in the shoot acts as a signal to regulate shoot-root allocation in tobacco. Plant J 1997, 11:671-691. Studies with plants expressing low levels of nitrate reductase implicate nitrate as a signal that controls many aspects of carbon and nitrogen metabolism.
2. 2 enrichment. New Phytologist 1996, 133:495-501. Intriguing finding that nitrogenous air pollutants increase nitrate reductase and nitrite reductase activities in leaves by pre-and post-translational mechanisms, raising the possibility that plants might use atmospheric nitrogen monoxide and nitrogen dioxide for plant growth.
3. Scheible WR, Gonzalez-Fontes A, Morcuende R, Lauerer M, Geiger M, Glaab J, Gojon A, Schulze ED, Stitt M: Tobacco mutants with a decreased number of functional nia genes compensate by modifying the diurnal regulation of transcription, post-translational modification and turnover of nitrate reductase. Planta 1997, 203:304-319. Paper describing evidence of mechanistic links among different levels of control of nitrate reductase.
4. Toroser D, Huber SC: Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves. Plant Physiol 1997, 114:947-955. Further characterization of the protein kinases responsible for inactivation of sucrose-phosphate synthase, and the identification of a distinct protein kinase that activates SPS. This makes SPS the first plant enzyme that has been demonstrated to be regulated by multisite phosphorylation.
5. Moorhead G, Douglas P, Morrice N, Scarabel M, Aitken A, Mackintosh C: Phosphorylated nitrate reductase is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr Biol 1996, 6:1104-1113. This paper, along with [6], shows that the inhibitor of phosphorylated nitrate reductase comprises one or more 14-3-3 isoforms [see 8], and that the interaction between nitrate reductase and 14-3-3 proteins can be prevented by competition with a phosphopeptide containing one of the phosphopeptide motifs on mammalian Raf-1 that bind 14-3-3 proteins.
6. Bachmann M, Huber JL, Liao P-C, Gage DA, Huber SC: The inhibitor of phosphorylated nitrate reductase from spinach (Spinacea oleracea) is a 14-3-3 protein. FEBS Lett 1996, 387:127-131. This paper, along with [5], identifies the inhibitor of phosphorylated nitrate reductase as a member of the 14-3-3 protein family.
7. Bachmann M, Huber JL, Athwal GS, Wu K, Ferl RJ, Huber SC: 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett 1996, 398:26-30. Further evidence that the 14-3-3 proteins bind directly to the phosphopeptide motif in the hinge 1 region of nitrate reductase, and that one consequence of 14-3-3 binding is to make the site less accessible to dephosphorylation.
8. Wu K, Rooney MF, Ferl RJ: The Arabidopsis 14-3-3 multigene family. Plant Physiol 1997, 114:1421-1431. Structural relationships among 10 isoforms of 14-3-3 proteins identified in Arabidopsis.