Literature DB >> 12516872

Metabolic enzymes as targets for 14-3-3 proteins.

Steven C Huber1, Carol MacKintosh, Werner M Kaiser.   

Abstract

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.

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Year:  2002        PMID: 12516872     DOI: 10.1023/a:1021284002779

Source DB:  PubMed          Journal:  Plant Mol Biol        ISSN: 0167-4412            Impact factor:   4.076


  65 in total

1.  14-3-3 proteins interact with a 13-lipoxygenase, but not with a 9-lipoxygenase.

Authors:  W L Holtman; M R Roberts; B J Oppedijk; C Testerink; M J van Zeijl; M Wang
Journal:  FEBS Lett       Date:  2000-05-26       Impact factor: 4.124

2.  A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity.

Authors:  G Tzivion; Z Luo; J Avruch
Journal:  Nature       Date:  1998-07-02       Impact factor: 49.962

3.  14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules.

Authors:  C Vincenz; V M Dixit
Journal:  J Biol Chem       Date:  1996-08-16       Impact factor: 5.157

4.  Ser-534 in the hinge 1 region of Arabidopsis nitrate reductase is conditionally required for binding of 14-3-3 proteins and in vitro inhibition.

Authors:  K Kanamaru; R Wang; W Su; N M Crawford
Journal:  J Biol Chem       Date:  1999-02-12       Impact factor: 5.157

5.  14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1.

Authors:  T F Schultz; J Medina; A Hill; R S Quatrano
Journal:  Plant Cell       Date:  1998-05       Impact factor: 11.277

6.  Identification of the 14.3.3 zeta domains important for self-association and Raf binding.

Authors:  Z J Luo; X F Zhang; U Rapp; J Avruch
Journal:  J Biol Chem       Date:  1995-10-06       Impact factor: 5.157

7.  The gdcsPA gene from Flaveria pringlei (Asteraceae).

Authors:  H Bauwe; S Kopriva
Journal:  Plant Physiol       Date:  1995-02       Impact factor: 8.340

8.  Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.

Authors:  A J Muslin; J W Tanner; P M Allen; A S Shaw
Journal:  Cell       Date:  1996-03-22       Impact factor: 41.582

9.  Cytosolic glutamine synthetase and not nitrate reductase from the green alga Chlamydomonas reinhardtii is phosphorylated and binds 14-3-3 proteins.

Authors:  M Pozuelo; C MacKintosh; A Galván; E Fernández
Journal:  Planta       Date:  2001-01       Impact factor: 4.116

10.  Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase.

Authors:  M Bachmann; N Shiraishi; W H Campbell; B C Yoo; A C Harmon; S C Huber
Journal:  Plant Cell       Date:  1996-03       Impact factor: 11.277

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  40 in total

Review 1.  14-3-3 protein regulation of proton pumps and ion channels.

Authors:  Tom D Bunney; Paul W J van den Wijngaard; Albertus H de Boer
Journal:  Plant Mol Biol       Date:  2002-12       Impact factor: 4.076

2.  Molecular mechanism of 14-3-3 protein-mediated inhibition of plant nitrate reductase.

Authors:  Iris C Lambeck; Katrin Fischer-Schrader; Dimitri Niks; Juliane Roeper; Jen-Chih Chi; Russ Hille; Guenter Schwarz
Journal:  J Biol Chem       Date:  2011-12-13       Impact factor: 5.157

3.  Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions.

Authors:  Anna-Lisa Paul; Paul C Sehnke; Robert J Ferl
Journal:  Mol Biol Cell       Date:  2005-01-19       Impact factor: 4.138

4.  Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes.

Authors:  Ryoung Shin; Sophie Alvarez; Adrien Y Burch; Joseph M Jez; Daniel P Schachtman
Journal:  Proc Natl Acad Sci U S A       Date:  2007-04-02       Impact factor: 11.205

5.  Proteomic analysis of changes in pea roots caused by the apoptosis-inducing concentration of salicylic acid.

Authors:  I A Tarchevsky; V G Yakovleva; A M Egorova
Journal:  Dokl Biochem Biophys       Date:  2008 Sep-Oct       Impact factor: 0.788

6.  A comprehensive analysis of the 14-3-3 interactome in barley leaves using a complementary proteomics and two-hybrid approach.

Authors:  Peter J Schoonheim; Helena Veiga; Daniel da Costa Pereira; Giulia Friso; Klaas J van Wijk; Albertus H de Boer
Journal:  Plant Physiol       Date:  2006-12-15       Impact factor: 8.340

7.  Defense/stress responses activated by chitosan in sycamore cultured cells.

Authors:  Massimo Malerba; Paolo Crosti; Raffaella Cerana
Journal:  Protoplasma       Date:  2011-02-14       Impact factor: 3.356

Review 8.  Plant 14-3-3 proteins as spiders in a web of phosphorylation.

Authors:  Albertus H de Boer; Paula J M van Kleeff; Jing Gao
Journal:  Protoplasma       Date:  2012-08-29       Impact factor: 3.356

9.  Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins.

Authors:  Diego M Bustos; Alberto A Iglesias
Journal:  Plant Physiol       Date:  2003-12       Impact factor: 8.340

10.  Comparative transcriptional survey between laser-microdissected cells from laminar abscission zone and petiolar cortical tissue during ethylene-promoted abscission in citrus leaves.

Authors:  Javier Agustí; Paz Merelo; Manuel Cercós; Francisco R Tadeo; Manuel Talón
Journal:  BMC Plant Biol       Date:  2009-10-23       Impact factor: 4.215

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