Literature DB >> 15032850

14-3-3 proteins: regulation of signal-induced events.

Robert J. Ferl1.   

Abstract

The field of signal transduction has experienced a significant paradigm shift as a result of an increased understanding of the roles of 14-3-3 proteins. There are many cases where signal-induced phosphorylation itself may cause a change in protein function. This simple modification is, in fact, the primary basis of signal transduction events in many systems. There are a large and growing number of cases, however, where simple phosphorylation is not enough to effect a change in protein function. In these cases, the 14-3-3 proteins can be required to complete the change in function. Therefore signal transduction can be either the relatively simple process where phosphorylation alters target activity, or it can be a more complex, multistep process with the 14-3-3 proteins playing the major role of bringing the signal transduction event to completion. This makes 14-3-3-modulated signal transduction a more complicated process with additional avenues for regulation and variety. Adding further complexity to the process is the fact that 14-3-3 proteins are present as multigene families in most organisms (Aitken et al. Trends Biochem Sci 17: 498-501, 1992; Ferl Annu Rev Plant Physiol Plant Molecular Biology 47: 49-73, 1996), with each member of the family being differentially expressed in various tissues and with potentially differential affinity for various target proteins. This review focuses on the 14-3-3 family of Arabidopsis as a model for further developing understanding of the roles of the 14-3-3 proteins as modulators of signal transduction events in plants. The primary approaches to these questions are not unlike the approaches that would be used in the functional dissection of any multigene family, but the interpretation of these data will have wide implications since the 14-3-3 s physically interact with other protein families.

Entities:  

Year:  2004        PMID: 15032850     DOI: 10.1111/j.0031-9317.2004.0239.x

Source DB:  PubMed          Journal:  Physiol Plant        ISSN: 0031-9317            Impact factor:   4.500


  22 in total

1.  Phototropism: mechanism and outcomes.

Authors:  Ullas V Pedmale; R Brandon Celaya; Emmanuel Liscum
Journal:  Arabidopsis Book       Date:  2010-08-31

2.  Combinations of SPR and MS for characterization of native and recombinant proteins in cell lysates.

Authors:  Jonas Borch; Peter Roepstorff
Journal:  Mol Biotechnol       Date:  2006-07       Impact factor: 2.695

3.  Expression profiling of the 14-3-3 gene family in response to salt stress and potassium and iron deficiencies in young tomato (Solanum lycopersicum) roots: analysis by real-time RT-PCR.

Authors:  Wei Feng Xu; Wei Ming Shi
Journal:  Ann Bot       Date:  2006-08-30       Impact factor: 4.357

Review 4.  Identifying protein interactors in gonadotropin action.

Authors:  James A Dias; Cheryl A Nechamen; Raghad Atari
Journal:  Endocrine       Date:  2005-04       Impact factor: 3.633

5.  14-3-3 isoforms participate in red light signaling and photoperiodic flowering.

Authors:  Kevin M Folta; Anna-Lisa Paul; John D Mayfield; Robert J Ferl
Journal:  Plant Signal Behav       Date:  2008-05

6.  Interaction of a 14-3-3 protein with the plant microtubule-associated protein EDE1.

Authors:  Cristina Pignocchi; John H Doonan
Journal:  Ann Bot       Date:  2011-05       Impact factor: 4.357

7.  Extracellular proteins in pea root tip and border cell exudates.

Authors:  Fushi Wen; Hans D VanEtten; George Tsaprailis; Martha C Hawes
Journal:  Plant Physiol       Date:  2006-12-01       Impact factor: 8.340

8.  Sequence analysis and transcriptional profiling of two vacuolar H+ -pyrophosphatase isoforms in Vitis vinifera.

Authors:  Mauritz Venter; Jan-Hendrik Groenewald; Frederik C Botha
Journal:  J Plant Res       Date:  2006-08-19       Impact factor: 2.629

9.  Sugar starvation- and GA-inducible calcium-dependent protein kinase 1 feedback regulates GA biosynthesis and activates a 14-3-3 protein to confer drought tolerance in rice seedlings.

Authors:  Shin-Lon Ho; Li-Fen Huang; Chung-An Lu; Siou-Luan He; Chun-Chin Wang; Sheng-Ping Yu; Jychian Chen; Su-May Yu
Journal:  Plant Mol Biol       Date:  2013-01-18       Impact factor: 4.076

10.  Phosphorylation of serine 1137/1138 of mouse insulin receptor substrate (IRS) 2 regulates cAMP-dependent binding to 14-3-3 proteins and IRS2 protein degradation.

Authors:  Sabine S Neukamm; Jennifer Ott; Sascha Dammeier; Rainer Lehmann; Hans-Ulrich Häring; Erwin Schleicher; Cora Weigert
Journal:  J Biol Chem       Date:  2013-04-24       Impact factor: 5.157

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