Impaired chaperone-mediated autophagy leads to abnormal SORT1 (sortilin 1) turnover and CES1-dependent triglyceride hydrolysis.

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Tác giả: You-Jin Choi, Byung Woo Han, Ji Ye Hyun, Byung-Hoon Lee, Wonseok Lee, Yewon Mun, Yoon Ah Nam, Cheon Jun Park, Jihyeon Yu, Sung Ho Yun

Ngôn ngữ: eng

Ký hiệu phân loại:

Thông tin xuất bản: United States : Autophagy , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 720219

SORT1 (sortilin 1), a member of the the Vps10 (vacuolar protein sorting 10) family, is involved in hepatic lipid metabolism by regulating very low-density lipoprotein (VLDL) secretion and facilitating the lysosomal degradation of CES1 (carboxylesterase 1), crucial for triglyceride (TG) breakdown in the liver. This study explores whether SORT1 is targeted for degradation by chaperone-mediated autophagy (CMA), a selective protein degradation pathway that directs proteins containing KFERQ-like motifs to lysosomes via LAMP2A (lysosomal-associated membrane protein 2A). Silencing LAMP2A or HSPA8/Hsc70 with siRNA increased cytosolic SORT1 protein levels. Leupeptin treatment induced lysosomal accumulation of SORT1, unaffected by si
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