The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons. (https://pubmed.ncbi.nlm.nih.gov/38383789/)

These scientists wanted to understand how a specific protein called UFM1 modifies another protein called RPL26 on ribosomes in our cells. They found that this modification, called UFMylation, is important for releasing ribosomes that get stuck at a part of the cell called the endoplasmic reticulum (ER). To figure out how this process works, the scientists used a powerful microscope to look at the structure of the UFM1 ribosome E3 ligase (UREL) complex, which is responsible for adding the UFM1 protein to the ribosomes.

They discovered that UREL wraps around the ribosomes in a specific way that blocks certain parts of the ribosome where other molecules would normally bind. This blocking action helps in releasing the ribosomes from the ER membrane. Without a properly working UREL, the ribosomes would stay stuck at the ER, causing problems in the cell. The scientists also found that UREL can switch its role from adding the UFM1 protein to recognizing the modified ribosomes, which is crucial for the release process.

In simple terms, these scientists studied how a special protein helps in releasing ribosomes that are stuck in a part of the cell, and they figured out the important role of this process in maintaining a healthy balance of proteins in our cells.

Makhlouf L., Peter JJ., Magnussen HM., Thakur R., Millrine D., Minshull TC., Harrison G., Varghese J., Lamoliatte F., Foglizzo M., Macartney T., Calabrese AN., Zeqiraj E., Kulathu Y. The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons. Nature. 2024 Feb 21. doi: 10.1038/s41586-024-07093-w.