UFMylation, it’s quite a strange word! What is it exactly?
It’s a type of post-translational modification (PTM), or a modification of a protein that occurs after it is translated by the ribosome. Post-translational modifications help to expand the functionality of the proteome. PTMs – which include things like the addition of chemical functional groups, conjugation to other peptides, or cleavage by proteases – affect protein structure, function, and protein-protein interactions (1).
Ubiquitination, a common PTM, involves the conjugation of a ubiquitin peptide (shown below) to another protein or peptide (the substrate) and is one of the most common PTMs around. UFMylation is ubiquitination’s cousin, as this process involves the conjugation of UFM1 (ubiquitin fold modifier 1), a small ubiquitin-like molecule, to a substrate.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7602216/
Many substrates of UFMylation have been discovered, including proteins like CYB5R3 (cytochrome B5 reductase 3 [2]), UFBP1 (UFM1 binding protein 1), RPL26 (ribosomal protein L26), and others (3; for additional information about each of these substrates and their modification by UFM1, check out each respective source!). Both the ubiquitination and UFMylation pathways (sometimes referred to as cascades) involve three specific enzyme types: E1 (activating), E2 (conjugating), and E3 (ligase) enzymes, eventually leading to conjugation of the peptide to its substrate (shown below).
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7602216/
PTMs are important cellular processes that affect other downstream processes. Without these modifications, cells would look and act quite differently. UFMylation is an interesting and relatively new PTM that is the topic of much current research!
Works Cited
(1) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8040245/
Science with Mandy 
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