Ca/calmodulin-mediated desensitization of glutamate receptors shapes plant systemic wound signalling and anti-herbivore defence.

Plants rely on systemic signalling mechanisms to establish whole-body defence in response to insect and nematode attacks. GLUTAMATE RECEPTOR-LIKE (GLR) genes have been implicated in long-distance transmission of wound signals to initiate the accumulation of the defence hormone jasmonate (JA) at undamaged distal sites. The systemic signalling entails the activation of Ca-permeable GLR channels by wound-released glutamate, triggering membrane depolarization and cytosolic Ca influx throughout the whole plant.

RALF signaling pathway activates MLO calcium channels to maintain pollen tube integrity.

Pollen tube tip growth requires intricate Ca signaling. Recent studies have also identified rapid alkalization factor (RALF)-family peptides and their receptors as critical components for pollen tube tip growth and integrity. The functional relationship of RALF and calcium signaling modules remains largely unclear.

A receptor-channel trio conducts Ca signalling for pollen tube reception.

Precise signalling between pollen tubes and synergid cells in the ovule initiates fertilization in flowering plants. Contact of the pollen tube with the ovule triggers calcium spiking in the synergids that induces pollen tube rupture and sperm release. This process, termed pollen tube reception, entails the action of three synergid-expressed proteins in Arabidopsis: FERONIA (FER), a receptor-like kinase; LORELEI (LRE), a glycosylphosphatidylinositol-anchored protein; and NORTIA (NTA), a transmembrane protein of unknown function.

Peroxymonosulfate activation by Co-doped magnetic MnO for degradation of oxytetracycline in water.

Co-doped magnetic MnO was synthesized by the solvothermal method and adopted as an effective catalyst for the degradation of oxytetracycline (OTC) in water. Synergistic interactions between Co-MnO and FeO not only resulted in the enhanced catalytic activity through the activation of peroxymonosulfate (PMS) to degrade OTC but also made FeO/Co-MnO easy to be separated and recovered from aqueous solution. 94.

Recent Advances in Genome-wide Analyses of Plant Potassium Transporter Families.

Plants require potassium (K) as a macronutrient to support numerous physiological processes. Understanding how this nutrient is transported, stored, and utilized within plants is crucial for breeding crops with high K use efficiency. As K is not metabolized, cross-membrane transport becomes a rate-limiting step for efficient distribution and utilization in plants.

A plasma membrane transporter coordinates phosphate reallocation and grain filling in cereals.

Phosphate (Pi) is essential to plant growth and crop yield. However, it remains unknown how Pi homeostasis is maintained during cereal grain filling. Here, we identified a rice grain-filling-controlling PHO1-type Pi transporter, OsPHO1;2, through map-based cloning.

Two glutamate- and pH-regulated Ca channels are required for systemic wound signaling in .

Plants defend against herbivores and nematodes by rapidly sending signals from the wounded sites to the whole plant. We investigated how plants generate and transduce these rapidly moving, long-distance signals referred to as systemic wound signals. We developed a system for measuring systemic responses to root wounding in We found that root wounding or the application of glutamate to wounded roots was sufficient to trigger root-to-shoot Ca waves and slow wave potentials (SWPs).

Calcium spikes, waves and oscillations in plant development and biotic interactions.

The calcium ion (Ca) is a universal signal in all eukaryotic cells. A fundamental question is how Ca, a simple cation, encodes complex information with high specificity. Extensive research has established a two-step process (encoding and decoding) that governs the specificity of Ca signals.

Cyclic nucleotide-gated channel 18 functions as an essential Ca channel for pollen germination and pollen tube growth in Arabidopsis.

We recently revealed that cyclic nucleotide-gated channel 18 (CNGC18) functioned as the main Ca channel in pollen tube tips for pollen tube guidance to ovules by regulating external Ca influx in Arabidopsis. In this study, we found that the reduction of external Ca concentration ([Ca]) from 10 mM to 5 mM, and further to 2 mM, led to the decreases of pollen germination percentages, but led to the increases of the percentages of ruptured pollen grains and tubes, and branched pollen tubes in vitro in cngc18-17 compared with wild type. The second point mutant allele cngc18-22 showed similar phenotypes, including reduced pollen germination percentages, increased percentages of ruptured pollen tubes, but did not show obvious different percentages of ruptured pollen grains and branched pollen tubes compared with wild type.

Cyclic nucleotide-gated channel 18 is an essential Ca2+ channel in pollen tube tips for pollen tube guidance to ovules in Arabidopsis.

In flowering plants, pollen tubes are guided into ovules by multiple attractants from female gametophytes to release paired sperm cells for double fertilization. It has been well-established that Ca(2+) gradients in the pollen tube tips are essential for pollen tube guidance and that plasma membrane Ca(2+) channels in pollen tube tips are core components that regulate Ca(2+) gradients by mediating and regulating external Ca(2+) influx. Therefore, Ca(2+) channels are the core components for pollen tube guidance.

Protein kinase OsSAPK8 functions as an essential activator of S-type anion channel OsSLAC1, which is nitrate-selective in rice.

OsSAPK8 is an essential activator of OsSLAC1 by phosphorylation, and OsSLAC1 is a nitrate-selective anion channel. S-type anion channel AtSLAC1 and protein kinase AtOST1 have been well-characterized as two core components of ABA signaling cascade in Arabidopsis guard cells, and AtOST1 functions as a main upstream activator of AtSLAC1 for drought stress- and ABA-induced stomata closure. However, the identity of the ortholog of AtOST1 in rice, the main activator of OsSLAC1, is still unknown.