EVI/WLS function is regulated by ubiquitination and linked to ER-associated degradation by ERLIN2

Wolf, Lucie; Lambert, Annika; Haenlin, Julie; Boutros, Michael

doi:10.1101/2020.12.09.417667

Cited by 3 publications

(1 citation statement)

References 70 publications

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“…First, Jean-Paul Vincent (The Francis Crick Institute, UK) discussed mechanisms underlying Wnt gradient formation (McGough et al, 2020). Then, Michael Boutros (German Cancer Research Center, Germany) talked about ERAD-mediated regulation of Evi/Wls protein, which is specifically involved in secretion of Wnt proteins (Wolf et al, 2021). David M. Virshup (Duke-NUS Medical School, Singapore) described telocyte-mediated delivery of Wnt ligands in the intestinal stem cell niche, and Steffen Scholpp (University of Exeter, UK) presented cytoneme-mediated transport of active Wnt5b/Ror2 complexes in zebrafish (Brunt et al, 2021).…”

Section: Oral Presentationsmentioning

confidence: 99%

Wnt 2022 EMBO | the Company of Biologists workshop and Yamada conference

et al. 2023

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Wnt2022 was held on November 15th-19th, 2022, in Awaji Yumebutai International Conference Center, Hyogo Prefecture, Japan, as an in-person meeting for the first time in last 3 years. Wnt signaling is a highly conserved pathway among various species. Since Wnt1 was discovered in 1982, a number of studies using many model animals and human samples have revealed that Wnt signaling plays crucial roles in embryonic development, tissue morphogenesis, and regeneration, as well as many other physiological and pathological processes. Since the year 2022 marks the 40th anniversary of Wnt research, we aimed to look back at our research progress and discuss the future direction of this field. The scientific program consisted of plenary lectures, invited talks, short talks selected from abstracts, and poster sessions. Whereas several different Wnt meetings have been held almost every year in Europe and the United States, this was the first Wnt meeting convened in Asia. Therefore, Wnt2022 was highly anticipated to bring together leaders and young scientists from Europe, the United States, and especially Asia and Oceania. In fact, 148 researchers from 21 countries attended this meeting. Although there were travel and administrative restrictions due to COVID-19, the meeting was highly successful in enabling face-to-face discussions.

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Section: Oral Presentationsmentioning

confidence: 99%

Wnt 2022 EMBO | the Company of Biologists workshop and Yamada conference

et al. 2023

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ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway

Veronese,

Kallabis,

Kaczmarek

et al. 2024

Preprint

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Complexes of ERLIN1 and ERLIN2 form large ring-like cup-shaped structures on the endoplasmic reticulum (ER) membrane and serve as platforms to bind cholesterol and E3-ubiquitin ligases, potentially defining functional nanodomains. Here, we show that ERLIN scaffolds mediate the interaction between the full-length isoform of TMUB1 and RNF170. We identify a luminal N-terminal conserved region in TMUB1 and RNF170 required for this interaction. Three-dimensional modelling shows that this conserved motif binds the SPFH domain of two adjacent ERLIN subunits at different interfaces. Protein variants that preclude these interactions have been previously linked to hereditary spastic paraplegia (HSP). By using omics approaches in combination with phenotypic characterisation of cells lacking both ERLINs, we demonstrate a role for ERLIN scaffolds in maintaining cholesterol levels in the ER by favouring transport to the Golgi over esterification, thereby regulating Golgi morphology and the secretory pathway.

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The Targeting of Native Proteins to the Endoplasmic Reticulum-Associated Degradation (ERAD) Pathway: An Expanding Repertoire of Regulated Substrates

Kumari

Brodsky

2021

Biomolecules

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All proteins are subject to quality control processes during or soon after their synthesis, and these cellular quality control pathways play critical roles in maintaining homeostasis in the cell and in organism health. Protein quality control is particularly vital for those polypeptides that enter the endoplasmic reticulum (ER). Approximately one-quarter to one-third of all proteins synthesized in eukaryotic cells access the ER because they are destined for transport to the extracellular space, because they represent integral membrane proteins, or because they reside within one of the many compartments of the secretory pathway. However, proteins that mature inefficiently are subject to ER-associated degradation (ERAD), a multi-step pathway involving the chaperone-mediated selection, ubiquitination, and extraction (or “retrotranslocation”) of protein substrates from the ER. Ultimately, these substrates are degraded by the cytosolic proteasome. Interestingly, there is an increasing number of native enzymes and metabolite and solute transporters that are also targeted for ERAD. While some of these proteins may transiently misfold, the ERAD pathway also provides a route to rapidly and quantitatively downregulate the levels and thus the activities of a variety of proteins that mature or reside in the ER.

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EVI/WLS function is regulated by ubiquitination and linked to ER-associated degradation by ERLIN2

Cited by 3 publications

References 70 publications

Wnt 2022 EMBO | the Company of Biologists workshop and Yamada conference

Wnt 2022 EMBO | the Company of Biologists workshop and Yamada conference

ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway

The Targeting of Native Proteins to the Endoplasmic Reticulum-Associated Degradation (ERAD) Pathway: An Expanding Repertoire of Regulated Substrates

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