2014年9月2日 · Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit postprandial hypertriglyceridemia. Further analyses reveal that Sel1L is indispensable for the secretion of lipoprotein lipase (LPL), independent of its role in Hrd1-mediated ERAD and ER homeostasis.

2023年5月30日 · Our data demonstrate that SEL1L-HRD1 ERAD is a critical regulator of LPL biology by degrading misfolding LPL in the ER. If not cleared efficiently, these LPL forms aggregates in the ER,...

2023年6月5日 · 研究发现，LPL在内质网中的折叠主要受SEL1L-HRD1 ERAD控制。 ERAD可及时清除在内质网中错误折叠的LPL蛋白，从而确保正确折叠的LPL蛋白被正常分泌。

2024年1月22日 · Endoplasmic reticulum-associated degradation (ERAD) plays indispensable roles in many physiological processes; however, the nature of endogenous substrates remains largely...

Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit postprandial hypertriglyceridemia. Further analyses reveal that Sel1L is indispensable for the secretion of lipoprotein lipase (LPL), independent of its role in Hrd1-mediated ERAD and ER homeostasis.

研究发现，LPL在内质网中的折叠主要受SEL1L-HRD1 ERAD控制。 ERAD可及时清除在内质网中错误折叠的LPL蛋白，从而确保正确折叠的LPL蛋白被正常分泌。

2025年2月4日 · Protein misfolding and aggregation in the endoplasmic reticulum (ER) have been causally linked to a variety of human diseases. Two key pathways for eliminating misfolded proteins and aggregates in the ER are ER-associated …

2014年9月2日 · Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit postprandial hypertriglyceridemia. Further analyses reveal that Sel1L is indispensable for the secretion of lipoprotein lipase (LPL), independent of its role in Hrd1-mediated ERAD and ER homeostasis.

2023年5月4日 · Here we report that the SEL1L–HRD1 protein complex—the most conserved branch of ER-associated degradation (ERAD)—is a negative regulator of the STING innate immunity by ubiquitinating and...

2024年1月24日 · Endoplasmic reticulum-associated degradation (ERAD) plays indispensable roles in many physiological processes; however, the nature of endogenous substrates remains largely elusive. Here we report a proteomics strategy based on the intrinsic property of the SEL1L-HRD1 ERAD complex to identify endogenous ERAD substrates both in vitro and in vivo.