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

Sci. STKE, 31 October 2000
Vol. 2000, Issue 56, p. pe1
DOI: 10.1126/stke.2000.56.pe1

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

  1. Paul C. Sehnke and
  2. Robert J. Ferl
  1. The authors are at the Program in Molecular and Cellular Biology, Department of Horticultural Sciences, University of Florida, Fifield Hall, Gainesville, FL 32611, USA. E-mail: robferl{at}ufl.edu

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.

Citation:

P. C. Sehnke and R. J. Ferl, Plant 14-3-3s: Omnipotent Metabolic Phosphopartners?. Sci. STKE 2000, pe1 (2000).
Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882