Projects per year
Description
During co-translational translocation at the endoplasmic reticulum (ER), ribosomes can stall and become covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit RPL26 (uL24). This process, known as UFMylation, is mediated by the UFM1 Ribosome E3 Ligase (UREL) complex, comprised of UFL1, UFBP1, and CDK5RAP3. However, the functional consequences of UFMylation and catalytic mechanisms of UREL are unknown. Here, we present crosslinking-mass spectrometry (XL-MS) data of UREL bound to 60S ribosomes.
Date made available | 22 Mar 2024 |
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Publisher | ProteomeXchange |
Projects
- 1 Active
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Establishment of Cryo-EM Screening Facility At University Of Dundee (Equipment Grant)
Kulathu, Y. (Investigator), Labib, K. (Investigator), Masson, G. (Investigator), Moraga Gonzalez, I. (Investigator), Murray, D. (Investigator), Owen-Hughes, T. (Investigator), Stanley-Wall, N. (Investigator) & Wyatt, P. (Investigator)
1/12/21 → 31/12/26
Project: Research
Research output
- 1 Article
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The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons
Makhlouf, L., Peter, J. J., Magnussen, H. M., Thakur, R., Millrine, D., Minshull, T. C., Harrison, G., Varghese, J., Lamoliatte, F., Foglizzo, M., Macartney, T., Calabrese, A. N., Zeqiraj, E. (Lead / Corresponding author) & Kulathu, Y. (Lead / Corresponding author), 14 Mar 2024, In: Nature. 627, 8003, p. 437-444 8 p.Research output: Contribution to journal › Article › peer-review
Open AccessFile11 Citations (Scopus)169 Downloads (Pure)
Datasets
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LC-MS/MS analysis of ribosome UFMylation in vitro
Kulathu, Y. (Supervisor), University of Dundee, 22 Mar 2024
https://www.ebi.ac.uk/pride/archive/projects/PXD046991
Dataset