- Protein family review
- Open Access
© BioMed Central Ltd 2002
- Published: 27 June 2002
Multiple members of the 14-3-3 protein family have been found in all eukaryotes so far investigated, yet they are apparently absent from prokaryotes. The major native forms of 14-3-3s are homo- and hetero-dimers, the biological functions of which are to interact physically with specific client proteins and thereby effect a change in the client. As a result, 14-3-3s are involved in a vast array of processes such as the response to stress, cell-cycle control, and apoptosis, serving as adapters, activators, and repressors. There are currently 133 full-length sequences available in GenBank for this highly conserved protein family. A phylogenetic tree based on the conserved middle core region of the protein sequences shows that, in plants, the 14-3-3 family can be divided into two clearly defined groups. The core region encodes an amphipathic groove that binds the multitude of client proteins that have conserved 14-3-3-recognition sequences. The amino and carboxyl termini of 14-3-3 proteins are much more divergent than the core region and may interact with isoform-specific client proteins and/or confer specialized subcellular and tissue localization.
- Client Protein
- Nuclear Export Signal
- Stigma Papillar
- Conserve Core Region
- Differential Subcellular Localization
The 14-3-3 protein family is highly conserved and is represented throughout the eukaryotic branch of life. The proteins were discovered in 1967 during a study of the soluble acidic proteins of the mammalian brain  and were named on the basis of fraction number during DEAE-cellulose chromatography and location after starch gel electrophoresis. For 25 years, 14-3-3s were generally thought to reside exclusively in animal brain tissue and to be involved in the function of neurons. During this early period of research, 14-3-3s were characterized as a heterogeneous family of dimeric proteins with a monomer mass of 25-32 kDa and multiple isoelectric points. One of the first biochemical functions of the 14-3-3s to be identified was the activation of the neurotransmitter pathway enzymes tyrosine hydroxylase and tryptophan hydroxylase, in a reaction requiring calcium and the cAMP-dependent kinase or calmodulin-dependent protein kinase II . Once 14-3-3s were found in Arabidopsis thaliana , maize  and other plants, and in tissues other than the brain, however, perspectives on their presence and roles broadened, and now 14-3-3s have been found in every eukaryote that has been screened for their presence. The vast number of organisms containing 14-3-3s suggests that this family of proteins is involved in many important biological processes .
Genetic, cellular and functional information on Arabidopsis 14-3-3s
Gene accession number 
Pollen, stigma papillar cells
Stems, leaves, flowers
Phi ( )
Nm, Pm, Ct
Nm, Pm, Ct
N, Pm, Ct
Stems, leaves, flowers
Nm, Pm, Ct
N, Pm/Cw, Ct
Ne, Pm, Ct, Sg
Stems, roots, flowers
The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins. Extensive investigation of the 14-3-3 binding site of the mammalian serine/threonine kinase Raf-1 has produced a consensus sequence for 14-3-3-binding, RSxpSxP (in the single-letter amino-acid code, where x denotes any amino acid and p indicates that the next residue is phosphorylated)  which has been verified through peptide library screening . A common, but not exclusive, requirement of 14-3-3 ligands is the phosphorylation of a serine or threonine residue in the target sequence. The phosphorylated consensus sequence does not, however, fully represent every ligand that 14-3-3s can bind: they are also known to bind other non-phosphorylated sequences such as GHSL , and WLDLE . A common, but not exclusive, requirement of 14-3-3 ligands is the phosphorylation of a serine residue in the target sequence. For those client proteins whose target sequences undergo phosphorylation, the binding of 14-3-3s to the target is the major step of a signal-transduction event. Despite the simplicity of the binding-site requirements, a diverse array of proteins potentially interact with 14-3-3s; some reports suggest that as many as 20% of Arabidopsis proteins are clients for 14-3-3s .
The 14-3-3 dimerization interaction occurs between the amino-terminal helix H1 of one monomer and helices H3 and H4 of the opposing monomer; the high conservation of amino-acid sequence along helices H1 and H3 among various isoforms allows 14-3-3s to heterodimerize (Figure 3) [21,22]. Two identical or different client proteins can be bound simultaneously by the dimer. This dual interaction means that possible roles of 14-3-3s include acting as adapters capable of bringing disparate client proteins together or moving or rearranging two different regions of the same protein. An example of the potential role of 14-3-3 dimers as adapters comes from studies of 14-3-3s interacting with the plant plasma-membrane proton ATPase and the plant toxin fusicoccin . It has been suggested that the 14-3-3 dimer binds the carboxy-terminal autoinhibitory (C-TA) domain of the ATPase in the presence of magnesium, creating a binding site where fusicoccin can then interact . Once fusicoccin is bound, the complex of 14-3-3 and the ATPase is stabilized and the C-TA domain is displaced, allowing the ATPase to become fully active.
In general, 14-3-3s are distributed widely throughout the cell, supporting the argument that they are involved in multiple protein-protein interactions in a plethora of biological roles. There is, however, some differential subcellular localization, suggesting an element of specialization among specific isoforms. Localization data have been collected for eight of the Arabidopsis isoforms using isoform-specific antibodies and fusions of 14-3-3 to green fluorescent protein (GFP; Table 1). These data do not necessarily exhaust all possible locations for each isoform; instead, they support the idea that certain isoforms are recruited to distinct subcellular locations. The localization of 14-3-3 κ and υ was studied using carboxy-terminal GFP fusions in transgenic Arabidopsis . Fusions of κ with GFP tended to localize to the plasma membrane, whereas υ-GFP fusions tended to be found in the cytosol . Additional data collected using microscopy and immuno-cytochemistry of total nuclear extracts showed that at least five different forms of 14-3-3s are found in the nucleus . Chloroplast stromal extracts screened with isoform-specific antibodies showed that 14-3-3 μ and ε (members of the epsilon group) and 14-3-3 υ and ν (members of the non-epsilon group) were the only 14-3-3s prominently located in the chloroplast . The presence of the two non-epsilon members 14-3-3 ν and υ in the chloroplast suggests that these proteins, although located on distinct branches of the phylogenetic tree, may share similar roles and cellular locations . 14-3-3 ε and μ were also found in starch grains ; ε has also been found at the nuclear envelope during 14-3-3-GFP studies. GFP-ω fusion studies showed that 14-3-3 nuclear localization is regulated by the cell-cycle ; generally, 14-3-3-ω-GFP fusions were excluded from the nucleus, but they accumulated in the nucleus just after nuclear division and then relocated back out of the nucleus just before completion of cytokinesis . In addition, a nuclear export signal was identified in the 14-3-3s of the fission yeast Schizosaccharomyces pombe that is required (in concert with the Crm1 nuclear export machinery) for the shuttling of the mitosis-inducing protein Cdc25 out of the nucleus following DNA damage . Nuclear shuttling has emerged as an important biological role for 14-3-3s , and the nuclear export signal (I/LxxxLxxxLxL) is highly conserved in the 133 full-length 14-3-3 sequences currently available (Figures 1 and 3).
The 14-3-3s are also differentially expressed among tissues and organs (Table 1). Arabidopsis 1ψ, λ, μ, and ε are found in the leaves; ψ and λ are also expressed in the stems and flowers , and χ is expressed in pollen grains and stigma papillar cells . The fact that 14-3-3s are differentially expressed in various tissues and differentially localized in subcellular compartments adds a layer of complexity to the examination and determination of biological roles for 14-3-3s, a complexity that must be reconciled with the highly conserved nature of 14-3-3-target interactions.
The identification of mutants and the use of transgenic organisms have provided some insight into some of the biological roles and locations of some 14-3-3s. For instance, a mutation in the RAD24 protein, one of the two 14-3-3s in S. pombe, reduces the yeast's ability to keep DNA damage in check . In Saccharomyces cerevisiae, disruption of the 14-3-3 genes BMH1 and BMH2 creates a lethal phenotype that can be rescued by introducing 14-3-3 isoforms from Arabidopsis, Dictyostelium discoideum, or Homo sapiens . The Leonardo (14-3-3 ζ) protein of Drosophila melanogaster is known to regulate presynaptic function, and its mutation results in the death of mature embryos . Two transgenic Arabidopsis lines, one carrying an antisense construct against 14-3-3 μ and another against 14-3-3 ε show dramatic increases in starch production in leaves .
Various 14-3-3s in a variety of species have been found to interact with proteins involved in signal transduction (such as Raf-1 ), apoptosis (such as the Bcl2-related protein Bad ), cell-cycle control (such as Cdc25 ), starch synthesis , nitrogen metabolism , and ATP regulation (reviewed in ).
Initially, discoveries of 14-3-3s were almost coincidental in nature; in many cases their identification was serendipitous after investigating other biochemical questions. Once it became established that these proteins were ubiquitous, research was directed toward identifying the number and sequences of isoforms present in different species as well as determining their functional diversity. As more genomes are sequenced, experimental tasks will move towards elucidation of general roles as well as investigation of isoform-specific roles in order to address the implications of 14-3-3 family diversity within organisms. Such studies are key to understanding the current conundrum: the conservation of 14-3-3s throughout eukaryotes suggests that some central biological roles might be served by any 14-3-3 protein, yet the diversity of 14-3-3 isoforms argues for a multitude of specific roles. Indeed, some combination of both concepts might be the case, with some roles being served by any isoform, and other roles requiring isoform-specific interactions. In any case, all the current data suggest that interactions involving 14-3-3 proteins are critical for the correct function of higher-order biological systems.
The presence of 14-3-3 proteins in most, if not all, eukaryotic cells, but not in any prokaryotic cells, offers an interesting opportunity to study the early evolutionary history of this protein family and the concomitant development of eukaryotic regulatory processes.
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