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

被引:113
作者
de Boer, Albertus H. [1 ]
van Kleeff, Paula J. M. [1 ]
Gao, Jing [1 ]
机构
[1] Vrije Univ Amsterdam, Dept Biol Struct, Fac Earth & Life Sci, NL-1081 HV Amsterdam, Netherlands
关键词
14-3-3; Phosphorylation; Kinase; bZIP transcription factors; Flowering; Hormonal signaling; BRASSINOSTEROID SIGNAL-TRANSDUCTION; BZIP TRANSCRIPTIONAL ACTIVATOR; REPRESSION OFSHOOT GROWTH; PLASMA-MEMBRANE; TYROSINE PHOSPHORYLATION; SUBCELLULAR-LOCALIZATION; ARABIDOPSIS; KINASE; BINDING; 14-3-3-PROTEINS;
D O I
10.1007/s00709-012-0437-z
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Protein phosphorylation is essential for many aspects of plant growth and development. To fully modulate the activity of specific proteins after phosphorylation, interaction with members of the 14-3-3 family is necessary. 14-3-3 Proteins are important for many processes because they "assist" a wide range of target proteins with divergent functions. In this review, we will describe how plant 14-3-3 proteins are as spiders in a web of phosphorylation: they act as sensors for phospho-motifs, they themselves are phosphorylated with unknown consequences and they have kinases as target, where some of these phosphorylate 14-3-3 binding motifs in other proteins. Two specific classes of 14-3-3 targets, protein kinases and transcription factors of the bZIP and basic helix-loop-helix-like families, with important and diverse functions in the plant as a whole will be discussed. An important question to be addressed in the near future is how the interaction with 14-3-3 proteins has diverged, both structurally and functionally, between different members of the same protein family, like the kinases and transcription factors.
引用
收藏
页码:425 / 440
页数:16
相关论文
共 121 条
[1]   FD, a bZIP protein mediating signals from the floral pathway integrator FT at the shoot apex [J].
Abe, M ;
Kobayashi, Y ;
Yamamoto, S ;
Daimon, Y ;
Yamaguchi, A ;
Ikeda, Y ;
Ichinoki, H ;
Notaguchi, M ;
Goto, K ;
Araki, T .
SCIENCE, 2005, 309 (5737) :1052-1056
[2]   Arabidopsis AtNek2 Kinase is Essential and Associates with Microtubules [J].
Agueci, Francesco ;
Rutten, Twan ;
Demidov, Dmitri ;
Houben, Andreas .
PLANT MOLECULAR BIOLOGY REPORTER, 2012, 30 (02) :339-348
[3]   Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. [J].
Aitken, A .
PLANT MOLECULAR BIOLOGY, 2002, 50 (06) :993-1010
[4]   14-3-3 proteins: A historic overview [J].
Aitken, Alastair .
SEMINARS IN CANCER BIOLOGY, 2006, 16 (03) :162-172
[5]   Post-translational modification of 14-3-3 isoforms and regulation of cellular function [J].
Aitken, Alastair .
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 2011, 22 (07) :673-680
[6]   A proteomic analysis of 14-3-3 binding proteins from developing barley grains [J].
Alexander, RD ;
Morris, PC .
PROTEOMICS, 2006, 6 (06) :1886-1896
[7]   The Timing of Flowering [J].
Amasino, Richard M. ;
Michaels, Scott D. .
PLANT PHYSIOLOGY, 2010, 154 (02) :516-520
[8]   Enzyme co-localization in the pea leaf cytosol: 3-P-glycerate kinase, glyceraldehyde-3-P dehydrogenase, triose-P isomerase and aldolase [J].
Anderson, LE ;
Carol, AA .
PLANT SCIENCE, 2005, 169 (03) :620-628
[9]   Identification of Phosphoproteins in Arabidopsis thaliana Leaves Using Polyethylene Glycol Fractionation, Immobilized Metal-ion Affinity Chromatography, Two-Dimensional Gel Electrophoresis and Mass Spectrometry [J].
Aryal, Uma K. ;
Krochko, Joan E. ;
Ross, Andrew R. S. .
JOURNAL OF PROTEOME RESEARCH, 2012, 11 (01) :425-437
[10]   Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis [J].
Benschop, Joris J. ;
Mohammed, Shabaz ;
O'Flaherty, Martina ;
Heck, Albert J. R. ;
Slijper, Monique ;
Menke, Frank L. H. .
MOLECULAR & CELLULAR PROTEOMICS, 2007, 6 (07) :1198-1214