Plant 14-3-3s: Omnipotent Metabolic Phosphopartners?

Science's STKE  31 Oct 2000:
Vol. 2000, Issue 56, pp. pe1
DOI: 10.1126/stke.2000.56.pe1

You are currently viewing the abstract.

View Full Text


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.

View Full Text