Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 529488
Title The ER-Associated Degradation Adapter Protein Sel1L Regulates Triglyceride Metabolism via Lipoprotein Lipase
Author(s) Sha, Haibo; Francisco, Adams; Sun, Shengyi; Ehrhardt, Nicole; Xue, Zhen; Liu, Lei; Lawrence, Peter; Mattijssen, Frits; Gruber, Robert; Panhwar, Muhammad S.; Brenna, J.T.; Shi, Hang; Xue, Bingzhong; Kersten, Sander; Bensadoun, André; Péterfy, Miklòs; Long, Qiaoming; Qi, Ling
Department(s) Chair Nutrition Metabolism and Genomics
VLAG
Publication type Dataset
Publication year 2015
Keyword(s) GSE56918 - Mus musculus - PRJNA244933
Abstract Sel1L is an adaptor protein for the E3 ligase Hrd1 in the endoplasmic reticulum-associated degradation (ERAD), but its physiological role in a cell-type-specific manner remains unclear. Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit postprandial hypertriglyceridemia. Mechanistically, our data demonstrate a critical requirement of Sel1L for the secretion of lipoprotein lipase (LPL), independently of its role in Hrd1-mediated ERAD and ER homeostasis. Further biochemical analyses revealed that Sel1L physically interacts and stabilizes the LPL maturation complex consisted of LPL and lipase-maturation factor 1 (LMF1). In the absence of Sel1L, LPL is retained in the ER and prone to the formation of protein aggregates, which are degraded by autophagy-mediated degradation. The Sel1L-mediated control of LPL secretion is seen in other LPL-expressing cell types as well such as cardiac muscle and macrophages. Thus, our study reports a novel role of Sel1L in LPL secretion and systemic lipid metabolism.
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