Nature Communications, https://doi.org/10.1038/s41467-024-46903-7 

Abstract

Proteins containing a ubiquitin regulatory X (UBX) domain are cofactors ofCell Division Cycle 48 (CDC48) and function in protein quality control. How-ever, whether and how UBX-containing proteins participate in host–microbeinteractions remain unclear. Here we show that MoNLE1, an effector from thefungal pathogen Magnaporthe oryzae, is a core virulence factor that sup-presses rice immunity by specifically interfering with OsPUX8B.2. The UBXdomain of OsPUX8B.2 is required for its binding to OsATG8 and OsCDC48-6and controls its 26 S proteasome–dependent stability. OsPUX8B.2 andOsCDC48-6 positively regulate plant immunity against blast fungus, while thehigh-temperature tolerance heat-shock protein OsBHT, a putative cytoplasmicsubstrate of OsPUX8B.2–OsCDC48-6, negatively regulates defense againstblast infection. MoNLE1 promotes the nuclear migration and degradation ofOsPUX8B.2 and disturbs its association with OsBHT. Given the high con-servation of MoNLE1 among fungal isolates, plants with broad and durableblast resistance might be generated by engineering intracellular proteinsresistant to MoNLE1.

Nature Communications，IF=16

https://rdcu.be/dB6gj