Biomedical subjects

Fuminori Takahashi

Publications and source records attributed to Fuminori Takahashi.

7 recordsLinked to original sources

PubMed2025

The TaCEP15 peptide signaling cascade modulates primary root length and drought tolerance in wheat.

Drought stress poses an environmental challenge affecting crop yield. Small signaling peptides play crucial roles in the regulation of stress responses in plants. Here, we unveil that the TaCEP15 peptide interacts with the leucine-rich repeat receptor-like kinase TaCEPRL. Knockout of TaCEP15 or TaCEPRL increases primary root length and enhances drought tolerance in wheat. TaCEPRL interacts with and phosphorylates TaSnRK1α, leading to the degradation of TaSnRK1α. The presence of TaCEP15 intensifies the phosphorylation and degradation of TaSnRK1α. Consistently, overexpressing TaSnRK1α boosts primary root elongation and augments drought tolerance. In addition, we identify the transcription factor TabZIP9, which binds to the TaCEP15 promoter and suppresses its transcription. A-to-T substitution in the TaCEP15 promoter decreases the binding affinity of TabZIP9. As expected, transgenic plants with TabZIP9 knockout or overexpression exhibit noteworthy changes in primary root length and drought tolerance. Our findings shed light on the importance of the peptide signaling pathway in regulating primary root length and responding to drought stress in wheat.

Triticum↗

PubMed2006

Crosstalk between abiotic and biotic stress responses: a current view from the points of convergence in the stress signaling networks.

Plants have evolved a wide range of mechanisms to cope with biotic and abiotic stresses. To date, the molecular mechanisms that are involved in each stress has been revealed comparatively independently, and so our understanding of convergence points between biotic and abiotic stress signaling pathways remain rudimentary. However, recent studies have revealed several molecules, including transcription factors and kinases, as promising candidates for common players that are involved in crosstalk between stress signaling pathways. Emerging evidence suggests that hormone signaling pathways regulated by abscisic acid, salicylic acid, jasmonic acid and ethylene, as well as ROS signaling pathways, play key roles in the crosstalk between biotic and abiotic stress signaling.

Plant Diseases↗

PubMed2005

The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis.

ABI1 and ABI2 encode PP2C-type protein phosphatases and are thought to negatively regulate many aspects of abscisic acid (ABA) signaling, including stomatal closure in Arabidopsis. In contrast, SRK2E/OST1/SnRK2.6 encodes an Arabidopsis SnRK2 protein kinase and acts as a positive regulator in the ABA-induced stomatal closure. SRK2E/OST1 is activated by osmotic stress as well as by ABA, but the independence of the two activation processes has not yet been determined. Additionally, interaction between SRK2E/OST1 and PP2C-type phosphatases (ABI1 and ABI2) is not understood. In the present study, we demonstrated that the abi1-1 mutation, but not the abi2-1 mutation, strongly inhibited ABA-dependent SRK2E/OST1 activation. In contrast, osmotic stress activated SRK2E/OST1 even in abi1-1 and aba2-1 plants. The C-terminal regulatory domain of SRK2E/OST1 was required for its activation by both ABA and osmotic stress in Arabidopsis. The C-terminal domain was functionally divided into Domains I and II. Domain II was required only for the ABA-dependent activation of SRK2E/OST1, whereas Domain I was responsible for the ABA-independent activation. Full-length SRK2E/OST1 completely complemented the wilty phenotype of the srk2e mutant, but SRK2E/OST1 lacking Domain II did not. Domain II interacted with the ABI1 protein in a yeast two-hybrid assay. Our results suggested that the direct interaction between SRK2E/OST1 and ABI1 through Domain II plays a critical role in the control of stomatal closure.

Abscisic Acid↗

PubMed2005

Structural analysis of cDNAs coding for 4SNc-Tudor domain protein from fish and their expression in yellowtail organs.

We cloned complementary DNAs for 4SNc-Tudor protein (SN4TDR) from yellowtail (Seriola quinqueradiata), torafugu (Takifugu rubripes), and zebrafish (Danio rerio). This protein contains 4 staphylococcal nuclease domains at the N terminus followed by a Tudor domain. We also identified the 4SNc-Tudor proteins highly homologous to that in yellowtail from the Takifugu genomic database. According to the smart database, these fish proteins had an overlapping Tudor domain (smart00333) with a complete 5 SNc domain (smart00318). In addition, 2 possible translation start sites were observed at the 5' sequences in all 3 fish species. Northern blot analysis of different yellowtail organs showed that the full SN4TDR messenger RNA was approximately 4000 nucleotides long and that its expression was highest in liver and gallbladder, being about 2 to 5 times higher than in kidney, brain, ovary, and gills, and exceedingly low in spleen, heart, and muscle. A minor 2000-nucleotide transcript observed in kidney, spleen, and gallbladder, was attributable to an alternatively spliced variant of this gene. Total proteins extracted from yellowtail liver were fractionated by heparin affinity column chromatography and separated by sodium dodecylsulfate polyacrylamide gel electrophoresis. Analyses by SDS-PAGE and liquid chromatography with tandem mass spectroscopy identified the polypeptide encoded by SN4TDR as a single molecule of 102 kDa.

Amino Acid Sequence↗

PubMed2003

Probing the cell peripheral movements by optical trapping technique.

Swiss 3T3 fibroblasts cultured on a poly-L-lysine-coated coverslip was stimulated with 0.5 micro M phorbol myristate acetate, and the movements of the peripheral membranes were probed with a 1- micro m polystyrene bead held in an optical trap. The bead brought into contact with the cell edge occasionally moved away from and returned to the original position. The movement ranged over 100 nm and occurred mainly in one direction, suggesting that the protruding cell membrane pushed the bead. The maximum velocities derived from individual pairs of protrusive and withdrawal movements exhibited a correlation, which is consistent with the previous reports. Acceleration and deceleration occurred both in the protrusive and withdrawal phases, indicating that the movements were regulated. Movement of the membrane occurred frequently with an ensemble-averaged maximum speed of 23 nm/s at the trap stiffness of 0.024 pN/nm, but it was strongly suppressed when the trap stiffness was increased to 0.090 pN/nm. Correlation of the protrusive and withdrawal velocities and the acceleration and deceleration both in the protrusive and withdrawal phases can be explained by the involvement of myosin motor at least in the withdrawal process. However, the fact that the movements were suppressed at higher trap stiffness implies a stochastic nature in the creation of the gap between the peripheral cell membrane and the actin network underlying it.

3T3 Cells↗

PubMed2002

Fenton reaction is primarily involved in a mechanism of (-)-epigallocatechin-3-gallate to induce osteoclastic cell death.

To propose candidates for the prevention or treatment of osteoporosis, we have screened compounds naturally in food for their ability to regulate the differentiation and function of osteoclasts. One of the major green tea flavonoids, (-)-epigallocatechin-3-gallate (EGCG), was found to induce apoptotic cell death of osteoclast-like multinucleated cells after 24 h treatment in a dose-dependent manner (25-100 microM), whereas osteoblasts were not affected. In the present study, we report for the first time a novel cell-death-inducing mechanism triggered by EGCG. The induction of apoptosis by EGCG was suppressed by pretreatment of catalase or calcitonin. It was also suppressed by Fe(III) and Fe(II) chelators. Furthermore, EGCG promoted the reduction of Fe(III) into Fe(II), and the combination of EGCG/Fe(III)/H(2)O(2) induced single-strand DNA breakage in a cell free system. These results indicate that the Fenton reaction is primarily involved in EGCG-induced osteoclastic cell death.

Animals↗

PubMed2002

ABA-activated SnRK2 protein kinase is required for dehydration stress signaling in Arabidopsis.

Protein phosphorylation has pivotal roles in ABA and osmotic stress signaling in higher plants. Two protein phosphatase genes, ABI1 and ABI2, are known to regulate these signaling pathways in Arabidopsis: The identity of ABA-activated protein kinases required for the ABA signaling, however, remains to be elucidated. Here we demonstrate that two protein kinases, p44 and p42, were activated by ABA in Arabidopsis T87 cultured cells, and at least one protein kinase, p44, was activated not only by ABA but also by low humidity in Arabidopsis plants. Analysis of T-DNA knockout mutants and biochemical analysis using a specific antibody revealed that the p44 is encoded by a SnRK2-type protein kinase gene, SRK2E. The srk2e mutation resulted in a wilty phenotype mainly due to loss of stomatal closure in response to a rapid humidity decrease. ABA-inducible gene expression of rd22 and rd29B was suppressed in srk2e. These results show that SRK2E plays an important role in ABA signaling in response to water stress.

Abscisic Acid↗