Ubiquitylation of the ER-Shaping Protein Lunapark via the CRL3KLHL12 Ubiquitin Ligase Complex
Publication date
2020-05-19
Authors
Yuniati, Laurensia
Lauriola, Angela
Gerritsen, Manouk
Abreu, Susana
Ni, Eric
Tesoriero, Chiara
Onireti, Jacob O.
Low, Teck Yew
Heck, Albert J.R.
Vettori, Andrea
Editors
Advisors
Supervisors
Document Type
Article
Metadata
Show full item recordCollections
License
cc_by
Abstract
Yuniati et al. perform a proteomic screen to identify E3 substrates that are ubiquitylated at cellular membranes and find that the ER-shaping protein Lunapark is ubiquitylated by the CRL3KLHL12 ubiquitin ligase. They show that Lunapark binds mTORC1 and affects its activity, and defects in Lunapark ubiquitylation lead to neurodevelopmental defects.
Keywords
cullin-RING ligases, endoplasmic reticulum, ER three-way junction, Lunapark, lysosome, mTORC1, ubiquitin, General Biochemistry,Genetics and Molecular Biology
Citation
Yuniati, L, Lauriola, A, Gerritsen, M, Abreu, S, Ni, E, Tesoriero, C, Onireti, J O, Low, T Y, Heck, A J R, Vettori, A, Cardozo, T & Guardavaccaro, D 2020, 'Ubiquitylation of the ER-Shaping Protein Lunapark via the CRL3 KLHL12 Ubiquitin Ligase Complex', Cell Reports, vol. 31, no. 7, 107664, pp. 1-20. https://doi.org/10.1016/j.celrep.2020.107664