TY - JOUR
T1 - Metabolic enzymes as targets for 14-3-3 proteins
AU - Huber, Steven C.
AU - MacKintosh, Carol
AU - Kaiser, Werner M.
N1 - Funding Information:
Work in the SCH laboratory represents cooperative investigations of the USDA/ARS and the North Carolina Agricultural Research Service, Raleigh, NC 27695-7643, USA. This work was also supported in part by grants from the USDA-NRI (grant 2001-35318-10185) to S.C.H.; the Deutsche Forschungsgemein-schaft (SFB 251) and EU contract (BIO4 CT97 2231) to W.M.K.; and the European Union (BI04-CT97-32231), the MRC (UK) and BBSRC (UK) to C.M. Mention of a trademark or proprietary product does not constitute a guarantee or warranty of the product by the NC ARS or the USDA and does not imply its approval to the exclusion of other products that may also be suitable.
PY - 2002/12
Y1 - 2002/12
N2 - The 14-3-3 proteins are binding proteins that have been shown to interact with a wide array of enzymes involved in primary biosynthetic and energy metabolism in plants. In most cases, the significance of binding of the 14-3-3 protein is not known. However, most of the interactions are phosphorylation-dependent and most of the known binding partners are found in the cytosol, while some may also be localized to plastids and mitochondria. In this review, we examine the factors that may regulate the binding of 14-3-3s to their target proteins, and discuss their possible roles in the regulation of the activity and proteolytic degradation of enzymes involved in primary carbon and nitrogen metabolism.
AB - The 14-3-3 proteins are binding proteins that have been shown to interact with a wide array of enzymes involved in primary biosynthetic and energy metabolism in plants. In most cases, the significance of binding of the 14-3-3 protein is not known. However, most of the interactions are phosphorylation-dependent and most of the known binding partners are found in the cytosol, while some may also be localized to plastids and mitochondria. In this review, we examine the factors that may regulate the binding of 14-3-3s to their target proteins, and discuss their possible roles in the regulation of the activity and proteolytic degradation of enzymes involved in primary carbon and nitrogen metabolism.
KW - 14-3-3-affinity chromatography
KW - Divalent cations
KW - Glutamine synthetase
KW - NADH:nitrate reductase
KW - Polyamines
KW - Proteolytic degradation
KW - Sucrose-phosphate synthase
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U2 - 10.1023/A:1021284002779
DO - 10.1023/A:1021284002779
M3 - Review article
C2 - 12516872
AN - SCOPUS:0036914587
SN - 0167-4412
VL - 50
SP - 1053
EP - 1063
JO - Plant Molecular Biology
JF - Plant Molecular Biology
IS - 6
ER -