Literature DB >> 22926776

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

Albertus H de Boer1, Paula J M van Kleeff, Jing Gao.   

Abstract

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.

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Year:  2012        PMID: 22926776     DOI: 10.1007/s00709-012-0437-z

Source DB:  PubMed          Journal:  Protoplasma        ISSN: 0033-183X            Impact factor:   3.356


  118 in total

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Journal:  Biochim Biophys Acta       Date:  1997-09-12

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

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5.  Plant metabolism: enzyme regulation by 14-3-3 proteins.

Authors:  P C Sehnke; R J Ferl
Journal:  Curr Biol       Date:  1996-11-01       Impact factor: 10.834

6.  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

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Journal:  J Biol Chem       Date:  2010-12-09       Impact factor: 5.157

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3.  Phosphorylation of HopQ1, a type III effector from Pseudomonas syringae, creates a binding site for host 14-3-3 proteins.

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Journal:  Proc Natl Acad Sci U S A       Date:  2013-05-15       Impact factor: 11.205

7.  Identification and Expression Analyses of the Special 14-3-3 Gene Family in Papaya and its Involvement in Fruit Development, Ripening, and Abiotic Stress Responses.

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8.  14-3-3-Pred: improved methods to predict 14-3-3-binding phosphopeptides.

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10.  A 14-3-3 Family Protein from Wild Soybean (Glycine Soja) Regulates ABA Sensitivity in Arabidopsis.

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