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Publisher Correction: SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex

Liangguang Leo Lin
Huilun Helen Wang
Ling Qi
Amendments and CorrectionsOpen Access15 Apr 2024
Nature Communications

Volume: 15, P: 1
PAWH1 and PAWH2 are plant-specific components of an Arabidopsis endoplasmic reticulum-associated degradation complex

Endoplasmic reticulum (ER)-associated degradation (ERAD) removes misfolded proteins from the secretory pathway. Here the authors identify two plant-specific proteins in Arabidopsis, PAWH1 and PAWH2, that bind to and stabilise the ER-anchored ubiquitin ligase Hrd1.

Liangguang Lin
Congcong Zhang
Jianming Li
ResearchOpen Access02 Aug 2019
Nature Communications

Volume: 10, P: 1-13
Proteomic screens of SEL1L-HRD1 ER-associated degradation substrates reveal its role in glycosylphosphatidylinositol-anchored protein biogenesis

The nature of SEL1L-HRD1 ERAD substrates remains unclear. Here, the authors identified ~100 endogenous substrates, and showed that SEL1L-HRD1 ERAD is indispensable for the activity of GPI transamidase complex and the biogenesis of GPI-anchored proteins.

Xiaoqiong Wei
You Lu
Ling Qi
ResearchOpen Access22 Jan 2024
Nature Communications

Volume: 15, P: 1-16
The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes

Endoplasmic reticulum (ER)-associated degradation (ERAD) and ER-phagy are two central degradative mechanisms in the ER. Here the authors describe the sequence of events underlying the disposition of misfolded ER proteins by ERAD and ER-phagy.

Shuangcheng Alivia Wu
Chenchen Shen
Ling Qi
ResearchOpen Access30 May 2023
Nature Communications

Volume: 14, P: 1-17
SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex

The importance of the SEL1L-HRD1 interaction in vivo was unclear. Here, authors reported that SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex by recruiting the E2 enzyme UBE2J1 and DERLIN to HRD1.

Liangguang Leo Lin
Huilun Helen Wang
Ling Qi
ResearchOpen Access16 Feb 2024
Nature Communications

Volume: 15, P: 1-20
SEL1L–HRD1 endoplasmic reticulum-associated degradation controls STING-mediated innate immunity by limiting the size of the activable STING pool

Ji et al. report that under basal conditions the SEL1L–HRD1 complex for endoplasmic reticulum-associated degradation ubiquitinates and negatively regulates STING protein levels in the endoplasmic reticulum, hence its activation.

Yewei Ji
Yuan Luo
Ling Qi
ResearchOpen Access04 May 2023
Nature Cell Biology

Volume: 25, P: 726-739
Genome-wide screens identify SEL1L as an intracellular rheostat controlling collagen turnover

Mechanisms regulating collagen clearance may be useful for treating fibrosis. Here, the authors conducted functional genome-wide screens and found that collagen biosynthesis directly regulates collagen clearance via a noncanonical function of SEL1L.

Michael J. Podolsky
Benjamin Kheyfets
Kamran Atabai
ResearchOpen Access20 Feb 2024
Nature Communications

Volume: 15, P: 1-17

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Publisher Correction: SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex

PAWH1 and PAWH2 are plant-specific components of an Arabidopsis endoplasmic reticulum-associated degradation complex

Proteomic screens of SEL1L-HRD1 ER-associated degradation substrates reveal its role in glycosylphosphatidylinositol-anchored protein biogenesis

The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes

SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex

SEL1L–HRD1 endoplasmic reticulum-associated degradation controls STING-mediated innate immunity by limiting the size of the activable STING pool

Genome-wide screens identify SEL1L as an intracellular rheostat controlling collagen turnover

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