title: Plant 14-3-3s: omnipotent metabolic phosphopartners?
abstract: The accurate regulation of metabolism is crucial to the existence all organisms. The inappropriate activation of metabolic enzymes can waste precious energy; likewise, the failure to activate metabolic enzymes can disrupt homeostasis and lead to suboptimal cellular (and organismic) responses. Plants use several means to control their metabolic proteins, including a two-step process of protein phosphorylation and subsequent binding by phosphospecific binding proteins termed 14-3-3 proteins. Sehnke and Ferl discuss how 14-3-3 proteins regulate the activity of nitrate reductase and the H(+)-ATPase pump in plants, and compare the functions of 14-3-3 proteins in plants and animals.
authors.affiliation: Program in Molecular and Cellular Biology, Department of Horticultural Sciences, University of Florida, Gainesville, FL, USA. robferl@ufl.edu
authors.forename: P C
authors.initials: PC
authors.lastname: Sehnke
authors.forename: R J
authors.initials: RJ
authors.lastname: Ferl
mesh_terms: D048948:14-3-3 Proteins; D000818:Animals; D006801:Humans; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism* / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism* / Q000502:physiology
chemical_list: D048948:14-3-3 Proteins; D010940:Plant Proteins; D014446:Tyrosine 3-Monooxygenase