Fungi are an important group of microorganisms that play crucial roles in a variety of ecological and biotechnological processes. Fungi depend on intracellular protein trafficking, which involves moving proteins from their site of synthesis to the final destination within or outside the cell. The soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins are vital components of vesicle trafficking and membrane fusion, ultimately leading to the release of cargos to the target destination. The v-SNARE (vesicle-associated SNARE) Snc1 is responsible for anterograde and retrograde vesicle trafficking between the plasma membrane (PM) and Golgi. It allows for the fusion of exocytic vesicles to the PM and the subsequent recycling of Golgi-localized proteins back to the Golgi via three distinct and parallel recycling pathways. This recycling process requires several components, including a phospholipid flippase (Drs2-Cdc50), an F-box protein (Rcy1), a sorting nexin (Snx4-Atg20), a retromer submit, and the COPI coat complex. Snc1 interacts with exocytic SNAREs (Sso1/2, Sec9) and the exocytic complex to complete the process of exocytosis. It also interacts with endocytic SNAREs (Tlg1 and Tlg2) during endocytic trafficking. Snc1 has been extensively investigated in fungi and has been found to play crucial roles in various aspects of intracellular protein trafficking. When Snc1 is overexpressed alone or in combination with some key secretory components, it results in enhanced protein production. This article will cover the role of Snc1 in the anterograde and retrograde trafficking of fungi and its interactions with other proteins for efficient cellular transportation.

Autophagy, a conserved cellular recycling process, plays a crucial role in maintaining homeostasis under stress conditions. It also regulates the development and virulence of numerous filamentous fungi. In this study, we investigated the specific function of ATG8, a reliable autophagic marker, in the opportunistic pathogen Aspergillus flavus. To investigate the role of atg8 in A. flavus, the deletion and complemented mutants of atg8 were generated according to the homologous recombination principle. Deletion of atg8 showed a significant decrease in conidiation, spore germination, and sclerotia formation compared to the WT and atg8^C strains. Additionally, aflatoxin production was found severely impaired in the ∆atg8 mutant. The stress assays demonstrated that ATG8 was important for A. flavus response to oxidative stress. The fluorescence microscopy showed increased levels of reactive oxygen species in the ∆atg8 mutant cells, and the transcriptional result also indicated that genes related to the antioxidant system were significantly reduced in the ∆atg8 mutant. We further found that ATG8 participated in regulating the pathogenicity of A. flavus on crop seeds. These results revealed the biological role of ATG8 in A. flavus, which might provide a potential target for the control of A. flavus and AFB1 biosynthesis.

In order to improve dispersibility, polymerization characteristics, chemical stability, and magnetic flocculation performance, magnetic Fe₃O₄ is often assembled with multifarious polymers to realize a functionalization process. Herein, a typical three-dimensional configuration of hyperbranched amino acid polymer (HAAP) was employed to assemble it with Fe₃O₄, in which we obtained three-dimensional hyperbranched magnetic amino acid composites (Fe₃O₄@HAAP). The characterization of the Fe₃O₄@HAAP composites was analyzed, for instance, their size, morphology, structure, configuration, chemical composition, charged characteristics, and magnetic properties. The magnetic flocculation of kaolin suspensions was conducted under different Fe₃O₄@HAAP dosages, pHs, and kaolin concentrations. The embedded assembly of HAAP with Fe₃O₄ was constructed by the N–O bond according to an X-ray photoelectron energy spectrum (XPS) analysis. The characteristic peaks of –OH (3420 cm⁻¹), C=O (1728 cm⁻¹), Fe–O (563 cm⁻¹), and N–H (1622 cm⁻¹) were observed in the Fourier transform infrared spectrometer (FTIR) spectra of Fe₃O₄@HAAP successfully. In a field emission scanning electron microscope (FE-SEM) observation, Fe₃O₄@HAAP exhibited a lotus-leaf-like morphological structure. A vibrating sample magnetometer (VSM) showed that Fe₃O₄@HAAP had a relatively low magnetization (Ms) and magnetic induction (Mr); nevertheless, the ferromagnetic Fe₃O₄@HAAP could also quickly respond to an external magnetic field. The isoelectric point of Fe₃O₄@HAAP was at 8.5. Fe₃O₄@HAAP could not only achieve a 98.5% removal efficiency of kaolin suspensions, but could also overcome the obstacles induced by high-concentration suspensions (4500 NTU), high pHs, and low fields. The results showed that the magnetic flocculation of kaolin with Fe₃O₄@HAAP was a rapid process with a 91.96% removal efficiency at 0.25 h. In an interaction energy analysis, both the U_DLVO and U_EDLVO showed electrostatic repulsion between the kaolin particles in the condition of a flocculation distance of 30 nm. As Fe₃O₄@ HAAP was employed, kaolin particles could cross the energy barrier more easily; thus, the fine flocs and particles were destabilized and aggregated further. Rapid magnetic separation was realized under the action of an external magnetic field.