High impact information on LOC548257

• Transient co-expression of 14-3-3 RNAi constructs along with an ABA-responsive promoter showed that each 14-3-3 is functional in generating an ABA response [1].
• 14-3-3 adaptor proteins are intermediates in ABA signal transduction during barley seed germination [1].
• Proteins of the 14-3-3 family have well-defined functions as regulators of plant primary metabolism and ion homeostasis [1].
• As ABA prolongs the presence of 14-3-3 proteins in the elongating radicle, we tested whether 14-3-3s are instrumental in ABA action using RNA interference [1].
• Together with previous data showing that 14-3-3 proteins control the activity of the plasma membrane H(+)-ATPase, this makes 14-3-3 a prime candidate for molecular master regulator of the cellular osmo-pump [2].

Biological context of LOC548257

• Both types of channels are under the control of 14-3-3 proteins, known as integral components of signal transduction pathways and instrumental in FC action [2].
• Our results show a novel isoform-specific post-translational modification of 14-3-3 proteins that is regulated in a tissue-specific and developmental way [3].
• A 14-3-3 protein has been cloned and sequenced from a cDNA library constructed from mRNAs of mature pollen grains of Lilium longiflorum Thunb [4].
• Here we report the first evidence that plant 14-3-3 proteins are involved in the down-regulation of ion channels in the vacuolar membrane as well [5].
• In the early embryogenesis stage, 14-3-3 subcellular localization differed among dividing and non-dividing microspores and the microspore-derived multicellular structures showed a polarized expression pattern of 14-3-3C and a higher 14-3-3A signal in epidermis primordia [6].

Anatomical context of LOC548257

• Germination-related modifications of 14-3-3 proteins were observed in the cytosol and the microsomal fraction, but not in the nucleus [7].
• 14-3-3 was shown to be present in isolated plastids [8].

Associations of LOC548257 with chemical compounds

• Abscisic acid and 14-3-3 proteins control K channel activity in barley embryonic root [2].
• Single amino acid variation in barley 14-3-3 proteins leads to functional isoform specificity in the regulation of nitrate reductase [9].
• Further, using site directed mutagenesis, we identified a single amino acid variation (Gly versus Ser) in loop 8 of the 14-3-3 proteins that plays an important role in the observed isoform specificity [9].
• Using the patch-clamp technique we have demonstrated that 14-3-3 protein drastically reduces the current carried by SV channels [5].

Regulatory relationships of LOC548257

• Sucrose synthase activity was shown to be inhibited by exogenous 14-3-3 in a dosage-dependent manner [8].

Analytical, diagnostic and therapeutic context of LOC548257

• Using surface plasmon resonance, we show that the ability of 14-3-3A and the mutated version to inhibit NR activity correlates well with their binding affinity for the 14-3-3 binding motif in the NR protein, indicating involvement of this residue in ligand discrimination [9].
• First, immunoprecipitation experiments, using isoenzyme-specific monoclonal Lox antibodies, showed that 14-3-3 proteins co-precipitate with 13-Lox, but not with the 9-Lox from barley [10].
• Western blot and immunolocalization of three barley 14-3-3 isoforms, 14-3-3A, 14-3-3B and 14-3-3C were carried out using isoform-specific antibodies [6].
• Southern blot analysis suggests that only one 14-3-3 gene is present in the Dictyostelium genome [11].

References