 NBR1 is an important protein involved in the recognition of ubiquitilated protein aggregates for vacular degradation by macroautophagy. Upon exposure to intense light, it associates with photodamaged chloroplasts independently of ATG7, a core component of the canonical autophagy machinery. It then coats both the surface and interior of chloroplasts, followed by its direct engulfment into the central vacuole through a microautophagy type process. Removal of the cell folligomerization MPB1 domain of NBR1 enhances this process. Additionally, the delivery of NBR1-decorated chloroplasts into vacuoles requires the ubiquitin-binding UBA2 domain of NBR1, which is independent of the ubiquitin E3 ligase SP1 and PUB4, known to direct the ubiquitillation of chloroplast surface proteins. Compared to wild-type plants, NBR1 mutants have altered levels of a subset of chloroplast proteins and display abnormal chloroplast density and sizes upon highlight expos. This article was authored by Hanim Lee, Genuvergis Choco, Ariodna Gonzales Solis, and others. We are article.tv. Links in the description below.