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Endoplasmic reticulum–associated degradation regulates mitochondrial dynamics in brown adipocytes
Author(s) -
Zhangsen Zhou,
Mauricio Torres,
Haibo Sha,
Christopher J. Halbrook,
Françoise Van den Bergh,
Rachel B. Reinert,
Tatsuya Yamada,
Siwen Wang,
Yingying Luo,
Allen H. Hunter,
Chunqing Wang,
Thomas H. Sanderson,
Meilian Liu,
Aaron B. Taylor,
Hiromi Sesaki,
Costas A. Lyssiotis,
Jun Wu,
Sander Kersten,
Daniel Beard,
Ling Qi
Publication year - 2020
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aay2494
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , microbiology and biotechnology , mitochondrion , adipogenesis , protein degradation , biology , unfolded protein response , chemistry , mesenchymal stem cell
Organelle cross-talk Endoplasmic reticulum (ER)–associated degradation (ERAD) is a quality control mechanism that allows for targeted degradation of proteins in the ER. Zhouet al. found that a particular protein complex in ERAD, Sel1L-Hrd1, regulates the dynamics of another organelle, the mitochondrion, by altering ER-mitochondria contacts. Three-dimensional high-resolution imaging in brown adipocytes from cold-challenged mice revealed that defective ERAD led to the formation of enlarged and abnormally shaped mitochondria with perforating ER tubules. The authors explored the consequences of ERAD deficiency on mitochondrial function and thermogenesis, which provides insights into ERADmediated ER-mitochondrial cross-talk and advances our understanding of the physiological importance of interorganelle contact.Science , this issue p.54

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