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Title: Plant 14-3-3s: omnipotent metabolic phosphopartners? Author: Sehnke PC, Ferl RJ. Journal: Sci STKE; 2000 Oct 31; 2000(56):pe1. PubMed ID: 11752616. 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.[Abstract] [Full Text] [Related] [New Search]