Heavy metals in soil can inflict direct damage on plants growing within it, adversely affecting their growth height, root development, leaf area, and other physiological traits. To counteract the toxic impacts of heavy metals on plant growth and development, plants mitigate heavy metal stress through mechanisms such as metal chelation, vacuolar compartmentalization, regulation of transporters, and enhancement of antioxidant functions. WRKY transcription factors (TFs) play a crucial role in plant growth and development as well as in responses to both biotic and abiotic stresses; notably, heavy metal stress is classified as an abiotic stressor. An increasing number of studies have highlighted the significant role of WRKY proteins in regulating heavy metal stress across various levels. Upon the entry of heavy metal ions into plant root cells, the production of reactive oxygen species (ROS) is triggered, leading to the phosphorylation and activation of WRKY TFs through MAPK cascade signaling. Activated WRKY TFs then modulate various physiological processes by upregulating or downregulating the expression of downstream genes to confer heavy metal tolerance to plants. This review provides an overview of the research advancements regarding WRKY TFs in regulating heavy metal ion stress—including cadmium (Cd), arsenic (As), copper (Cu)—and aluminum (Al) toxicity.

The homotypic fusion and protein sorting (HOPS) complex is a conserved, multi-subunit tethering complex in eukaryotic cells. In yeast and mammalian cells, the HOPS subunit vacuolar protein sorting-associated protein 41 (VPS41) is recruited to late endosomes after Ras-related protein 7 (Rab7) activation and is essential for vacuole fusion. However, whether VPS41 plays conserved roles in plants is not clear. Here, we demonstrate that in the model plant Arabidopsis (Arabidopsis thaliana), VPS41 localizes to distinct condensates in root cells in addition to its reported localization at the tonoplast. The formation of condensates does not rely on the known upstream regulators but depends on VPS41 self-interaction and is essential for vegetative growth regulation. Genetic evidence indicates that VPS41 is required for both homotypic vacuole fusion and cargo sorting from the adaptor protein complex 3, Rab5, and Golgi-independent pathways but is dispensable for the Rab7 cargo inositol transporter 1. We also show that VPS41 has HOPS-independent functions in vacuolar transport. Taken together, our findings indicate that Arabidopsis VPS41 is a unique subunit of the HOPS complex that carries out plant-specific roles in both vacuolar transport and developmental regulation.

Post-translational modifications (PTMs) of proteins are involved in numerous biological processes, including signal transduction, cell cycle regulation, growth and development, and stress responses. WRKY transcription factors (TFs) play significant roles in plant growth, development, and responses to both biotic and abiotic stresses, making them one of the largest and most vital TF families in plants. Recent studies have increasingly highlighted the importance of PTMs of WRKY TFs in various life processes. This review focuses on the recent advancements in understanding the phosphorylation and ubiquitination of WRKY TFs, particularly their roles in resistance to biotic and abiotic stresses and in plant growth and development. Future research directions and prospects in this field are also discussed.

Throughout their life cycle, plants persistent through environmental adversities that activate sophisticated stress-signaling networks, with protein kinases serving as pivotal regulators of these responses. The sucrose non-fermenting-1-related protein kinase 2 (SnRK2), a plant-specific serine/threonine kinase, orchestrates stress adaptation by phosphorylating downstream targets to modulate gene expression and physiological adjustments. While SnRK2 substrates have been extensively identified, the existing literature lacks a systematic classification of these components and their functional implications. This review synthesizes recent advances in characterizing SnRK2-phosphorylated substrates in Arabidopsis thaliana, providing a mechanistic framework for their roles in stress signaling and developmental regulation. Furthermore, we explore the understudied paradigm of SnRK2 undergoing multilayered post-translational modifications (PTMs), including phosphorylation, ubiquitination, SUMOylation, S-nitrosylation, sulfation (S-sulfination and tyrosine sulfation), and N-glycosylation. These PTMs collectively fine-tune SnRK2 stability, activity, and subcellular dynamics, revealing an intricate feedback system that balances kinase activation and attenuation. By integrating substrate networks with regulatory modifications, this work highlights SnRK2’s dual role as both a phosphorylation executor and a PTM-regulated scaffold, offering new perspectives for engineering stress-resilient crops through targeted manipulation of SnRK2 signaling modules.