
USP8은 Rabex5와의 상호작용을 통해 엔도좀에 모집되어 Rabex5의 해리를 유도하고 SAND-1/Mon1의 모집을 촉진함으로써 엔도좀 성숙을 조절한다.


coremsg

The spatiotemporal transition of small GTPase Rab5 to Rab7 is crucial for early-to-late endosome maturation, yet the precise mechanism governing Rab5-to-Rab7 switching remains elusive. USP8, a ubiquitin-specific protease, plays a prominent role in the endosomal sorting of a wide range of transmembrane receptors and is a promising target in cancer therapy. Here, we identified that USP8 is recruited to Rab5-positive carriers by Rabex5, a guanine nucleotide exchange factor (GEF) for Rab5. The recruitment of USP8 dissociates Rabex5 from early endosomes (EEs) and meanwhile promotes the recruitment of the Rab7 GEF SAND-1/Mon1. In USP8-deficient cells, the level of active Rab5 is increased, while the Rab7 signal is decreased. As a result, enlarged EEs with abundant intraluminal vesicles (ILVs) accumulate and digestive lysosomes are rudimentary. Together, our results reveal an important and unexpected role of a deubiquitinating enzyme in endosome maturation.

### Competing Interest Statement

The authors have declared no competing interest.

Spatiotemporal recruitment of the ubiquitin-specific protease USP8 directs endosome maturation

usp8-의-시공간적-모집이-엔도좀-성숙을-주도한다


USP8 의 시공간적 모집이 엔도좀 성숙을 주도한다
