Retromer protein VPS29 plays a crucial and positive role in the sumoylation system mediated by E3 SUMO ligase SIZ1.

ABSTRACT: Vacuolar protein sorting 29 (VPS29) functions in retrograde protein transport as a component of the retromer complex. However, the role of VPS29 in the regulation of post-translational modifications, such as sumoylation and ubiquitination, has not been elucidated. In this study, we demonstrate that VPS29 positively regulates SIZ/PIAS-type E3 SUMO (Small ubiquitin-related modifier) ligase-mediated sumoylation systems. In Arabidopsis, vps29-3 mutants display upregulated salicylic acid (SA) signaling pathways and reactive oxygen species accumulation, similar to those observed in siz1 mutants. Arabidopsis VPS29 (AtVPS29) directly interacts with the Arabidopsis E3 SUMO ligase SIZ1 (AtSIZ1) and localizes not only to the cytoplasm but also to the nucleus. The loss of AtVPS29 leads to a depletion

SUBMITTER: Min WK 

PROVIDER: S-EPMC12033008 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature