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

Paul, Anna-Lisa / Sehnke, Paul C / Ferl, Robert J

2005 Volume 16, Issue 4, Page(s) 1735–1743

Abstract: In most higher eukaryotes, the predominantly phosphoprotein-binding 14-3-3 proteins are the products of a multigene family, with many organisms having 10 or more family members. However, current models for 14-3-3/phosphopeptide interactions suggest that ... ...

Abstract	In most higher eukaryotes, the predominantly phosphoprotein-binding 14-3-3 proteins are the products of a multigene family, with many organisms having 10 or more family members. However, current models for 14-3-3/phosphopeptide interactions suggest that there is little specificity among 14-3-3s for diverse phosphopeptide clients. Therefore, the existence of sequence diversity among 14-3-3s within a single organism begs questions regarding the in vivo specificities of the interactions between the various 14-3-3s and their clients. Chief among those questions is, Do the different 14-3-3 isoforms interact with different clients within the same cell? Although the members of the Arabidopsis 14-3-3 family of proteins typically contain highly conserved regions of sequence, they also display distinctive variability with deep evolutionary roots. In the current study, a survey of several Arabidopsis 14-3-3/GFP fusions revealed that 14-3-3s demonstrate distinct and differential patterns of subcellular distribution, by using trichomes and stomate guard cells as in vivo experimental cellular contexts. The effects of client interaction on 14-3-3 localization were further analyzed by disrupting the partnering with peptide and chemical agents. Results indicate that 14-3-3 localization is both isoform specific and highly dependent upon interaction with cellular clients.
MeSH term(s)	14-3-3 Proteins/genetics ; 14-3-3 Proteins/metabolism ; Aminoimidazole Carboxamide/analogs & derivatives ; Aminoimidazole Carboxamide/metabolism ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Transport ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Ribonucleotides/metabolism
Chemical Substances	14-3-3 Proteins ; Protein Isoforms ; Recombinant Fusion Proteins ; Ribonucleotides ; Aminoimidazole Carboxamide (360-97-4) ; AICA ribonucleotide (F0X88YW0YK)
Language	English
Publishing date	2005-04
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E04-09-0839
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Article: Proteomic analysis of the 14-3-3 family in Arabidopsis.

Fuller, Brian / Stevens, Stanley M / Sehnke, Paul C / Ferl, Robert J

Proteomics

2006 Volume 6, Issue 10, Page(s) 3050–3059

Abstract: In this study, various proteomics-based methods were utilized to examine the 14-3-3 protein family in Arabidopsis thaliana. A protein extract was prepared from an Arabidopsis hypocotyl suspension culture and analyzed by two-dimensional gel ... ...

Abstract	In this study, various proteomics-based methods were utilized to examine the 14-3-3 protein family in Arabidopsis thaliana. A protein extract was prepared from an Arabidopsis hypocotyl suspension culture and analyzed by two-dimensional gel electrophoresis and immunoblotting with a 14-3-3 monoclonal antibody that recognizes multiple Arabidopsis isoforms. Protein spots that cross-reacted with the monoclonal antibody as well as the surrounding spots were analyzed by high performance liquid chromatography in conjunction with electrospray-tandem mass spectrometry. Nine separate spots contained 14-3-3s and each spot contained multiple 14-3-3 isoforms. Every isoform observed was verified by the identification of at least one isoform-specific peptide. Further analysis by mass spectrometry revealed that the isoforms Chi, Upsilon, Omega, Phi, and Lambda were acetylated on their N termini and no non-acetylated N termini were recovered. These data, together with the distribution of isoforms and the confirmation that 14-3-3s are not complexed during urea denaturing isoelectric focusing, supports the conclusion that Arabidopsis 14-3-3s are acetylated in vivo and are significantly affected by other post-translational modifications.
MeSH term(s)	14-3-3 Proteins/metabolism ; Acetylation ; Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Electrophoresis, Gel, Two-Dimensional ; Hypocotyl/metabolism ; Protein Isoforms/metabolism ; Proteomics
Chemical Substances	14-3-3 Proteins ; Arabidopsis Proteins ; Protein Isoforms
Language	English
Publishing date	2006-05
Publishing country	Germany
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2032093-0
ISSN	1615-9861 ; 1615-9853
ISSN (online)	1615-9861
ISSN	1615-9853
DOI	10.1002/pmic.200500729
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Article: Remote sensing of gene expression in Planta: transgenic plants as monitors of exogenous stress perception in extraterrestrial environments.

Manak, Michael S / Paul, Anna-Lisa / Sehnke, Paul C / Ferl, Robert J

Life support & biosphere science : international journal of earth space

2002 Volume 8, Issue 2, Page(s) 83–91

Abstract: Transgenic arabidopsis plants containing the alcohol dehydrogenase (Adh) gene promoter fused to the green fluorescent protein (GFP) reporter gene were developed as biological sensors for monitoring physiological responses to unique environments. Plants ... ...

Abstract	Transgenic arabidopsis plants containing the alcohol dehydrogenase (Adh) gene promoter fused to the green fluorescent protein (GFP) reporter gene were developed as biological sensors for monitoring physiological responses to unique environments. Plants were monitored in vivo during exposure to hypoxia, high salt, cold, and abcissic acid in experiments designed to characterize the utility and responses of the Adh/GFP biosensors. Plants in the presence of environmental stimuli that induced the Adh promoter responded by expressing GFP, which in turn generated a detectable fluorescent signal. The GFP signal degraded when the inducing stimulus was removed. Digital imaging of the Adh/GFP plants exposed to each of the exogenous stresses demonstrated that the stress-induced gene expression could be followed in real time. The experimental results established the feasibility of using a digital monitoring system for collecting gene expression data in real time from Transgenic Arabidopsis Gene Expression System (TAGES) biosensor plants during space exploration experiments.
MeSH term(s)	Alcohol Dehydrogenase/genetics ; Arabidopsis/genetics ; Arabidopsis/physiology ; Biosensing Techniques ; Extraterrestrial Environment ; Gene Expression Regulation, Plant ; Genes, Reporter ; Green Fluorescent Proteins ; Image Processing, Computer-Assisted ; Luminescent Proteins/genetics ; Plant Physiological Phenomena ; Plants, Genetically Modified/genetics ; Plants, Genetically Modified/physiology ; Promoter Regions, Genetic ; Telemetry
Chemical Substances	Luminescent Proteins ; Green Fluorescent Proteins (147336-22-9) ; Alcohol Dehydrogenase (EC 1.1.1.1)
Language	English
Publishing date	2002
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1069-9422
ISSN	1069-9422
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Article: Exposed Loop Domains of Complexed 14-3-3 Proteins Contribute to Structural Diversity and Functional Specificity

Sehnke, Paul C / Laughner, Beth / Cardasis, Helene / Powell, David / Ferl, Robert J

Plant physiology. 2006 Feb., v. 140, no. 2

2006

Abstract: ... of the medial amino acid in the loop 8 domain changed the flexibility of the C terminus and altered client ...

Abstract	The 14-3-3 family of proteins functions through protein:phosphoprotein interactions, the nature of which has been elucidated using x-ray crystallography. However, some key structural features in nonconserved regions have yet to be fully resolved, leaving open questions regarding the functional selectivity of 14-3-3 family members for diverse clients. In an effort to study surface accessible structural features in 14-3-3 containing macromolecular complexes and to illuminate important structure/function variations among the 14-3-3 isoforms, we determined the epitopes for three unique monoclonal antibodies (mAbs) developed against the Arabidopsis (Arabidopsis thaliana) G-box DNA:protein complex. The epitopes mapped to different loops in a phylogenetically important subset of the 13 14-3-3 family members. All three epitopes were on a common exposed face of complexed 14-3-3s. Two of the mAbs recognized linear sequences within loops 5 and 6, while the third mAb recognized 14-3-3 residues surrounding the pivotal medial Gly in the divalent cation-binding domain of loop 8, together with distal residue(s) in the putative dynamic 10th helix that has yet to be determined by crystallography. Gly at this loop 8 position is unique to nonepsilon 14-3-3 isoforms of the plant kingdom, suggesting that this region constitutes a plant-specific key functional 14-3-3 feature and highlighting that the loop 8 region is functionally significant. Mutagenesis of the medial amino acid in the loop 8 domain changed the flexibility of the C terminus and altered client peptide-binding selectivity, demonstrating the functional significance of the surface accessible, evolutionarily distinct loop 8 domain.
Keywords	Arabidopsis thaliana ; plant proteins ; protein isoforms ; protein structure ; molecular models ; cross reaction ; monoclonal antibodies ; Western blotting ; epitopes ; plant biochemistry ; amino acid sequences
Language	English
Dates of publication	2006-02
Size	p. 647-660.
Document type	Article
ZDB-ID	208914-2
ISSN	1532-2548 ; 0032-0889
ISSN (online)	1532-2548
ISSN	0032-0889
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Article: Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity.

Sehnke, Paul C / DeLille, Justin M / Ferl, Robert J

The Plant cell

2002 Volume 14 Suppl, Page(s) S339–54

MeSH term(s)	14-3-3 Proteins ; Arabidopsis/genetics ; Arabidopsis/physiology ; Gene Expression Regulation, Plant/drug effects ; Nitrates/pharmacology ; Phylogeny ; Plant Proteins/genetics ; Plant Proteins/physiology ; Protein Sorting Signals ; Proteome/metabolism ; Signal Transduction/physiology ; Stress, Mechanical ; Tyrosine 3-Monooxygenase/genetics ; Tyrosine 3-Monooxygenase/physiology
Chemical Substances	14-3-3 Proteins ; Nitrates ; Plant Proteins ; Protein Sorting Signals ; Proteome ; Tyrosine 3-Monooxygenase (EC 1.14.16.2) ; ammonium nitrate (T8YA51M7Y6)
Language	English
Publishing date	2002-01-30
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Review
ZDB-ID	623171-8
ISSN	1532-298X ; 1040-4651
ISSN (online)	1532-298X
ISSN	1040-4651
DOI	10.1105/tpc.010430
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Article: Exposed loop domains of complexed 14-3-3 proteins contribute to structural diversity and functional specificity.

Sehnke, Paul C / Laughner, Beth / Cardasis, Helene / Powell, David / Ferl, Robert J

Plant physiology

2006 Volume 140, Issue 2, Page(s) 647–660

Abstract: ... of the medial amino acid in the loop 8 domain changed the flexibility of the C terminus and altered client ...

Abstract	The 14-3-3 family of proteins functions through protein:phosphoprotein interactions, the nature of which has been elucidated using x-ray crystallography. However, some key structural features in nonconserved regions have yet to be fully resolved, leaving open questions regarding the functional selectivity of 14-3-3 family members for diverse clients. In an effort to study surface accessible structural features in 14-3-3 containing macromolecular complexes and to illuminate important structure/function variations among the 14-3-3 isoforms, we determined the epitopes for three unique monoclonal antibodies (mAbs) developed against the Arabidopsis (Arabidopsis thaliana) G-box DNA:protein complex. The epitopes mapped to different loops in a phylogenetically important subset of the 13 14-3-3 family members. All three epitopes were on a common exposed face of complexed 14-3-3s. Two of the mAbs recognized linear sequences within loops 5 and 6, while the third mAb recognized 14-3-3 residues surrounding the pivotal medial Gly in the divalent cation-binding domain of loop 8, together with distal residue(s) in the putative dynamic 10th helix that has yet to be determined by crystallography. Gly at this loop 8 position is unique to nonepsilon 14-3-3 isoforms of the plant kingdom, suggesting that this region constitutes a plant-specific key functional 14-3-3 feature and highlighting that the loop 8 region is functionally significant. Mutagenesis of the medial amino acid in the loop 8 domain changed the flexibility of the C terminus and altered client peptide-binding selectivity, demonstrating the functional significance of the surface accessible, evolutionarily distinct loop 8 domain.
MeSH term(s)	14-3-3 Proteins/chemistry ; 14-3-3 Proteins/immunology ; 14-3-3 Proteins/metabolism ; Amino Acid Sequence ; Antibodies, Monoclonal/metabolism ; Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/immunology ; Arabidopsis Proteins/metabolism ; Binding Sites ; Blotting, Western ; Epitope Mapping ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptide Library ; Phosphopeptides/metabolism ; Phylogeny ; Protein Isoforms/chemistry ; Protein Isoforms/immunology ; Protein Isoforms/metabolism ; Protein Structure, Tertiary ; Sequence Alignment ; Substrate Specificity
Chemical Substances	14-3-3 Proteins ; Antibodies, Monoclonal ; Arabidopsis Proteins ; Peptide Library ; Phosphopeptides ; Protein Isoforms
Language	English
Publishing date	2006-01-11
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	208914-2
ISSN	1532-2548 ; 0032-0889
ISSN (online)	1532-2548
ISSN	0032-0889
DOI	10.1104/pp.105.073916
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Article: Identification and characterization of GIP1, an Arabidopsis thaliana protein that enhances the DNA binding affinity and reduces the oligomeric state of G-box binding factors.

Sehnke, Paul C / Laughner, Beth J / Lyerly Linebarger, Carla R / Gurley, William B / Ferl, Robert J

Cell research

2005 Volume 15, Issue 8, Page(s) 567–575

Abstract: Environmental control of the alcohol dehydrogenase (Adh) and other stress response genes in plants is in part brought about by transcriptional regulation involving the G-box cis-acting DNA element and bZIP G-box Binding Factors (GBFs). The mechanisms of ... ...

Abstract	Environmental control of the alcohol dehydrogenase (Adh) and other stress response genes in plants is in part brought about by transcriptional regulation involving the G-box cis-acting DNA element and bZIP G-box Binding Factors (GBFs). The mechanisms of GBF regulation and requirements for additional factors in this control process are not well understood. In an effort to identify potential GBF binding and control partners, maize GBF1 was used as bait in a yeast two-hybrid screen of an A. thaliana cDNA library. GBF Interacting Protein 1 (GIP1) arose from the screen as a 496 amino acid protein with a predicted molecular weight of 53,748 kDa that strongly interacts with GBFs. Northern analysis of A. thaliana tissue suggests a 1.8-1.9 kb GIP1 transcript, predominantly in roots. Immunolocalization studies indicate that GIP1 protein is mainly localized to the nucleus. In vitro electrophoretic mobility shift assays using an Adh G-box DNA probe and recombinant A. thaliana GBF3 or maize GBF1, showed that the presence of GIP1 resulted in a tenfold increase in GBF DNA binding activity without altering the migration, suggesting a transient association between GIP1 and GBF. Addition of GIP1 to intentionally aggregated GBF converted GBF to lower molecular weight macromolecular complexes and GIP1 also refolded denatured rhodanese in the absence of ATP. These data suggest GIP1 functions to enhance GBF DNA binding activity by acting as a potent nuclear chaperone or crowbar, and potentially regulates the multimeric state of GBFs, thereby contributing to bZIP-mediated gene regulation.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Cell Nucleus/metabolism ; DNA/metabolism ; DNA, Complementary/genetics ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Electrophoretic Mobility Shift Assay ; Gene Expression Regulation, Plant ; Genomics ; Molecular Chaperones/metabolism ; Molecular Sequence Data ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Plant Roots/genetics ; Protein Binding ; Protein Structure, Quaternary ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/immunology ; Two-Hybrid System Techniques ; Zea mays
Chemical Substances	Arabidopsis Proteins ; Carrier Proteins ; DNA, Complementary ; DNA-Binding Proteins ; GIP1 protein, Arabidopsis ; Molecular Chaperones ; Multiprotein Complexes ; RNA, Messenger ; Recombinant Fusion Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2005-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1319303-x
ISSN	1748-7838 ; 1001-0602
ISSN (online)	1748-7838
ISSN	1001-0602
DOI	10.1038/sj.cr.7290326
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Article: FTICR-MS analysis of 14-3-3 isoform substrate selection.

Cardasis, Helene L / Sehnke, Paul C / Laughner, Beth / Eyler, John R / Powell, David H / Ferl, Robert J

Biochimica et biophysica acta

2007 Volume 1774, Issue 7, Page(s) 866–873

Abstract: The 14-3-3s are a ubiquitous class of eukaryotic proteins that participate in a second regulatory step in many phosphorylation-based signal transduction systems. The Arabidopsis family of 14-3-3 proteins represents a rather large 14-3-3 gene family. The ... ...

Abstract	The 14-3-3s are a ubiquitous class of eukaryotic proteins that participate in a second regulatory step in many phosphorylation-based signal transduction systems. The Arabidopsis family of 14-3-3 proteins represents a rather large 14-3-3 gene family. The biological motive for such diversity within a single protein family is not yet completely understood. The work presented here utilizes 14-3-3 micro-affinity chromatography in conjunction with Fourier transform ion cyclotron resonance mass spectrometry to survey the substrate sequence selectivity of two Arabidopsis 14-3-3 isoforms that represent the two major subclasses of this protein family. A method was developed to compare the relative binding of eight synthetic phosphopeptide sequences. The degree to which each phosphopeptide bound to either isoform was assigned a relative value, defined here as the binding ratio. The method provided a simple means for visualizing differences in substrate sequence selection among different 14-3-3 isoforms. A reproducible preference for specific phosphopeptide sequences was measured for both isoforms. This binding preference was consistent among the two classes of isoforms, suggesting that any pressure for isoform selectivity must reside outside the central core that interacts with the phosphopeptide sequence of the client.
MeSH term(s)	14-3-3 Proteins/chemistry ; Arabidopsis/metabolism ; Biochemistry/methods ; Biophysics/methods ; Chromatography, Affinity/methods ; Mass Spectrometry/methods ; Peptides/chemistry ; Phosphopeptides/chemistry ; Phosphorylation ; Plant Proteins/chemistry ; Protein Binding ; Protein Isoforms ; Spectroscopy, Fourier Transform Infrared/methods ; Substrate Specificity
Chemical Substances	14-3-3 Proteins ; Peptides ; Phosphopeptides ; Plant Proteins ; Protein Isoforms
Language	English
Publishing date	2007-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2007.05.004
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Article: Plasma membrane H(+)-ATPase and 14-3-3 isoforms of Arabidopsis leaves: evidence for isoform specificity in the 14-3-3/H(+)-ATPase interaction.

Alsterfjord, Magnus / Sehnke, Paul C / Arkell, Annika / Larsson, Håkan / Svennelid, Fredrik / Rosenquist, Magnus / Ferl, Robert J / Sommarin, Marianne / Larsson, Christer

Plant & cell physiology

2004 Volume 45, Issue 9, Page(s) 1202–1210

Abstract: The plasma membrane H(+)-ATPase is activated by binding of 14-3-3 protein to the phosphorylated C ...

Abstract	The plasma membrane H(+)-ATPase is activated by binding of 14-3-3 protein to the phosphorylated C terminus. Considering the large number of 14-3-3 and H(+)-ATPase isoforms in Arabidopsis (13 and 11 expressed genes, respectively), specificity in binding may exist between 14-3-3 and H(+)-ATPase isoforms. We now show that the H(+)-ATPase is the main target for 14-3-3 binding at the plasma membrane, and that all twelve 14-3-3 isoforms tested bind to the H(+)-ATPase in vitro. Using specific antibodies for nine of the 14-3-3 isoforms, we show that GF14epsilon, mu, lambda, omega, chi, phi, nu, and upsilon are present in leaves, but that isolated plasma membranes lack GF14chi, phi and upsilon. Northern blots using isoform-specific probes for all 14-3-3 and H(+)-ATPase isoforms showed that transcripts were present for most of the isoforms. Based on mRNA levels, GF14epsilon, mu, lambda and chi are highly expressed 14-3-3 isoforms, and AHA1, 3, and 11 highly expressed H(+)-ATPase isoforms in leaves. However, mass peptide fingerprinting identified AHA1 and 2 with the highest score, and their presence could be confirmed by MS/MS. It may be calculated that under 'unstressed' conditions less than one percent of total 14-3-3 is attached to the H(+)-ATPase. However, during a condition requiring full activation of H+ pumping, as induced here by the presence of the fungal toxin fusicoccin, several percent of total 14-3-3 may be engaged in activation of the H(+)-ATPase.
MeSH term(s)	14-3-3 Proteins/metabolism ; Arabidopsis/enzymology ; Arabidopsis/metabolism ; Cell Membrane/enzymology ; Electrophoresis, Polyacrylamide Gel ; Isoenzymes/metabolism ; Plant Leaves/enzymology ; Plant Leaves/metabolism ; Protein Isoforms/metabolism ; Proton-Translocating ATPases/metabolism ; Substrate Specificity
Chemical Substances	14-3-3 Proteins ; Isoenzymes ; Protein Isoforms ; Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2004-09
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	208907-5
ISSN	1471-9053 ; 0032-0781
ISSN (online)	1471-9053
ISSN	0032-0781
DOI	10.1093/pcp/pch136
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Article: Evolution and isoform specificity of plant 14-3-3 proteins.

Sehnke, Paul C / Rosenquist, Magnus / Alsterfjord, Magnus / DeLille, Justin / Sommarin, Marianne / Larsson, Christer / Ferl, Robert J

Plant molecular biology

2002 Volume 50, Issue 6, Page(s) 1011–1018

Abstract: The 14-3-3 proteins, once thought of as obscure mammalian brain proteins, are fast becoming recognized as major regulators of plant primary metabolism and of other cellular processes. Their presence as large gene families in plants underscores their ... ...

Abstract	The 14-3-3 proteins, once thought of as obscure mammalian brain proteins, are fast becoming recognized as major regulators of plant primary metabolism and of other cellular processes. Their presence as large gene families in plants underscores their essential role in plant physiology. We have examined the Arabidopsis thaliana 14-3-3 gene family, which currently is the largest and most complete 14-3-3 family with at least 12 expressed members and 15 genes from the now completed Arabidopsis thaliana genome project. The phylogenetic branching of this family serves as the prototypical model for comparison with other large plant 14-3-3 families and as such may serve to rationalize clustering in a biological context. Equally important for ascribing common functions for the various 14-3-3 isoforms is determining an isoform-specific correlation with localization and target partnering. A summary of localization information available in the literature is presented. In an effort to identify specific 14-3-3 isoform location and participation in cellular processes, we have produced a panel of isoform-specific antibodies to Arabidopsis thaliana 14-3-3s and present initial immunolocalization studies that suggest biologically relevant, discriminative partnering of 14-3-3 isoforms.
MeSH term(s)	14-3-3 Proteins ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Evolution, Molecular ; Microscopy, Fluorescence ; Phylogeny ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Tyrosine 3-Monooxygenase/genetics ; Tyrosine 3-Monooxygenase/metabolism
Chemical Substances	14-3-3 Proteins ; Plant Proteins ; Protein Isoforms ; Tyrosine 3-Monooxygenase (EC 1.14.16.2)
Language	English
Publishing date	2002-08-16
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	778032-1
ISSN	1573-5028 ; 0167-4412
ISSN (online)	1573-5028
ISSN	0167-4412
DOI	10.1023/a:1021289127519
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