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RILP Induces Cholesterol Accumulation in Lysosomes by Inhibiting Endoplasmic Reticulum–Endolysosome Interactions

Published:6 August 2024 DOI: 10.3390/cells13161313 PMID: 39195203
Yang Han,?Xiaoqing Liu,?Liju Xu,?Ziheng Wei,?Yueting Gu,?Yandan Ren,?Wenyi Hua,?Yongtao Zhang,?Xiaoxi Liu,?Cong Jiang,?Ruijuan Zhuang,?Wanjin Hong,?Tuanlao Wang

Abstract

Endoplasmic reticulum (ER)-endolysosome interactions regulate cholesterol exchange between the ER and the endolysosome. ER-endolysosome membrane contact sites mediate the ER-endolysosome interaction. VAP-ORP1L (vesicle-associated membrane protein-associated protein- OSBP-related protein 1L) interaction forms the major contact site between the ER and the lysosome, which is regulated by Rab7. RILP (Rab7-interacting lysosomal protein) is the downstream effector of Rab7, but its role in the organelle interaction between the ER and the lysosome is not clear. In this study, we found RILP interacts with ORP1L to competitively inhibit the formation of the VAP-ORP1L contact site. Immunofluorescence microscopy revealed that RILP induces late endosome/lysosome clustering, which reduces the contact of endolysosomes with the ER, interfering with the ER-endolysosome interaction. Further examination demonstrated that over-expression of RILP results in the accumulation of cholesterol in the clustered endolysosomes, which triggers cellular autophagy depending on RILP. Our results suggest that RILP interferes with the ER-endolysosome interaction to inhibit cholesterol flow from the endolysosome to the ER, which feedbacks to trigger autophagy.

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Torin 1 1222998-36-8 C35H28F3N5O2 194 suppliers $28.00-$4500.00
Torin 1 1222998-36-8 C35H28F3N5O2 194 suppliers $28.00-$4500.00
Torin 1 1222998-36-8 C35H28F3N5O2 194 suppliers $28.00-$4500.00
Torin 1 1222998-36-8 C35H28F3N5O2 194 suppliers $28.00-$4500.00

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