Recently, Prof. Meng Li’ group from the Institute for Advanced Study at Shenzhen University published a research article in theCell Reports, making a breakthrough in research on archaea evolution and eukaryogenesis. This work characterizes the role of a UEV-Vps23 protein family in functional interplay between endosomal sorting complexes required for transport and ubiquitin system in Asgard archaea. The Prof. Li is the corresponding author, and the first authors are Zhongyi Lu, Siyu Zhang, and Prof. Yang Liu.

Functional interplay between the endosomal sorting complexes required for transport (ESCRT) and ubiquitin system underlines ubiquitin-dependent protein cargo-sorting pathway of eukaryotic endomembrane system, yet its evolutionary origin remains poorly understood. This work shows that the UEV-Vps23 contains UEV and Vps23 domains. The UEV binds ubiquitin, making the UEV-Vps23 a sensor for sorting ubiquitinated cargo. The Vps23 domains can undergo ubiquitination by Asgard ubiquitin system. Interaction between the UEV and Vps23 domain leads to autoinhibited form, regulating the ESCRT and ubiquitin system interplay in Asgard archaea. In addition, the results of phylogenetic analysis, sequence comparison, and structural modelling indicate that the Asgard UEV-Vps23, eukaryotic Vps23, and archaeal CdvA share a common evolutionary origin.

This work was supported by the Natural Science Foundation of China (32225003，32393970，32393971，92251306，32370004), Guangdong Basic and Applied Basic Research Foundation (2023A1515011309) and Shenzhen University 2035 Program for Excellent Research (2022B002). Link to the article:https://doi.org/10.1016/j.celrep.2024.113781。

Figure 1 Evolution and mechanism of Asgard archaeal UEV-Vps23.