No abstract

The perception and relay of cell-wall signals are critical for plants to regulate growth and stress responses, but the underlying mechanisms are poorly understood. We found that the cell-wall leucine-rich repeat extensins (LRX) 3/4/5 are critical for plant salt tolerance in Arabidopsis. The LRXs physically associate with the RAPID ALKALINIZATION FACTOR (RALF) peptides RALF22/23, which in turn interact with the plasma membrane-localized receptor-like protein kinase FERONIA (FER). The lrx345 triple mutant as well as fer mutant plants display retarded growth and salt hypersensitivity, which are mimicked by overexpression of RALF22/23. Salt stress promotes S1P protease-dependent release of mature RALF22 peptides. Treatment of roots with mature RALF22/23 peptides or salt stress causes the internalization of FER. Our results suggest that the LRXs, RALFs, and FER function as a module to transduce cell-wall signals to regulate plant growth and salt stress tolerance.

Additives treatment is as a very effective strategy to optimize bulk heterojunction (BHJ) morphology. However, the inherent working mechanism of this strategy still lacks systematical investigations in non‐fullerene‐acceptors‐based organic solar cells (OSCs). Herein, a series of BHJ and pseudo‐planar heterojunction (PPHJ) OSCs using PM6 and IT‐4F as the electron donor/acceptor pair, are developed to unveil the promoting effect of solvent additive 1, 8‐diiodooctane (DIO) on active layer morphologies and device performance. The study clearly demonstrates that DIO can increase the crystallinity of IT‐4F significantly, while it has less impact on PM6. It is notable that a new efficiency‐determining crystalline balanced factor (CCLpolymer/CCLacceptor) is put forward, indicating that the more balanced CCLpolymer/CCLacceptor results in more balanced charge mobility and much better short‐circuit current densities (Jsc) and fill factors (FF) of OSCs. The PPHJ blend film of PM6/IT‐4F(DIO) exhibits enhanced crystallinity with more balanced CCL and favorable hierarchical distribution morphology, contributing to a champion efficiency of 13.70% with a record Jsc of 20.98 mA cm−2 and a remarkable FF of 75.9%. This work not only reveals the underlying mechanism of DIO caused morphology evolution, but also achieves highly efficient PPHJ OSCs with superior thermal stability by elaborately controlling the morphology of PPHJ film.

Protein kinases are major regulatory components in almost all cellular processes in eukaryotic cells. By adding phosphate groups, protein kinases regulate the activity, localization, protein–protein interactions, and other features of their target proteins. It is known that protein kinases are central components in plant responses to environmental stresses such as drought, high salinity, cold, and pathogen attack. However, only a few targets of these protein kinases have been identified. Moreover, how these protein kinases regulate downstream biological processes and mediate stress responses is still largely unknown. In this study, we introduce a strategy based on isotope-labeled in vitro phosphorylation reactions using in vivo phosphorylated peptides as substrate pools and apply this strategy to identify putative substrates of nine protein kinases that function in plant abiotic and biotic stress responses. As a result, we identified more than 5,000 putative target sites of osmotic stress-activated SnRK2.4 and SnRK2.6, abscisic acid-activated protein kinases SnRK2.6 and casein kinase 1-like 2 (CKL2), elicitor-activated protein kinase CDPK11 and MPK6, cold-activated protein kinase MPK6, H2O2-activated protein kinase OXI1 and MPK6, and salt-induced protein kinase SOS1 and MPK6, as well as the low-potassium-activated protein kinase CIPK23. These results provide comprehensive information on the role of these protein kinases in the control of cellular activities and could be a valuable resource for further studies on the mechanisms underlying plant responses to environmental stresses.

Summary The capability to maintain cell wall integrity is critical for plants to adapt to unfavourable conditions. l‐Arabinose (Ara) is a constituent of several cell wall polysaccharides and many cell wall‐localised glycoproteins, but so far the contribution of Ara metabolism to abiotic stress tolerance is still poorly understood. Here, we report that mutations in the MUR4 (also known as HSR8) gene, which is required for the biosynthesis of UDP‐Arap in Arabidopsis, led to reduced root elongation under high concentrations of NaCl, KCl, NaNO3, or KNO3. The short root phenotype of the mur4/hsr8 mutants under high salinity is rescued by exogenous Ara or gum arabic, a commercial product of arabinogalactan proteins (AGPs) from Acacia senegal. Mutation of the MUR4 gene led to abnormal cell−cell adhesion under salt stress. MUR4 forms either a homodimer or heterodimers with its isoforms. Analysis of the higher order mutants of MUR4 with its three paralogues, MURL, DUR, MEE25, reveals that the paralogues of MUR4 also contribute to the biosynthesis of UDP‐Ara and are critical for root elongation. Taken together, our work revealed the importance of the Ara metabolism in salt stress tolerance and also provides new insights into the enzymes involved in the UDP‐Ara biosynthesis in plants.