Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis

MacKintosh, C. and Meek, S.E.M. (2001) Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis. Cellular and Molecular Life Sciences, 58(2), pp. 205-214. (doi: 10.1007/PL00000848)

Abstract

This review highlights progress in dissecting how plant nitrate reductase (NR) activity is regulated by Ca2+, protein kinases, protein kinase kinases, protein phosphatases, 14-3-3 proteins and protease(s). The signalling components that regulate NR have also been discovered to target other enzymes of metabolism, vesicle trafficking and cellular signalling. Extracellular sugars exert a major impact on the 14-3-3-binding status and stability of many target proteins, including NR in plants, whereas other stimuli affect the regulation of some targets and not others. We thus begin to see how selective or global switches in cellular behaviour are triggered by regulatory networks in response to different environmental stimuli. Surprisingly, the question of how changes in NR activity actually affect the rate of nitrate assimilation is turning out to be a tough problem.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Meek, Dr Sarah and MacKintosh, Prof Carol
• Authors: MacKintosh, C., and Meek, S.E.M.
• College/School: College of Medical Veterinary and Life Sciences > School of Medicine, Dentistry & Nursing
• Journal Name: Cellular and Molecular Life Sciences
• Publisher: Birkhauser Verlag
• ISSN: 1420-682X
• ISSN (Online): 1420-9071