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Review
. 2020 Oct 14;10(10):1442.
doi: 10.3390/biom10101442.

Decrypting UFMylation: How Proteins Are Modified with UFM1

Sayanika Banerjee  1 , Manoj Kumar  1 , Reuven Wiener  1
Affiliations
Review

Decrypting UFMylation: How Proteins Are Modified with UFM1

Sayanika Banerjee et al. Biomolecules. .

Abstract

Besides ubiquitin (Ub), humans have a set of ubiquitin-like proteins (UBLs) that can also covalently modify target proteins. To date, less is known about UBLs than Ub and even less is known about the UBL called ubiquitin-fold modifier 1 (UFM1). Currently, our understanding of protein modification by UFM1 (UFMylation) is like a jigsaw puzzle with many missing pieces, and in some cases it is not even clear whether these pieces of data are in the right place. Here we review the current data on UFM1 from structural biology to biochemistry and cell biology. We believe that the physiological significance of protein modification by UFM1 is currently underestimated and there is more to it than meets the eye.

Keywords: UBA5; UFC1; UFL1; UFM1; UFMylation; conjugating enzymes; ubiquitin-like proteins.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Comparison between electrostatic potential surfaces of ubiquitin-fold modifier 1 (UFM1) (PDB id 5IA7) and ubiquitin (Ub) (PDB id 1UBQ). Upper panel: cartoon representation of the orientation of the indicated protein; lower panel: the corresponding electrostatic surface. The electrostatic potential surface was calculated using UCSF Chimera [13].
Figure 2
Figure 2
The UFM1 conjugation pathway. The figure depicts the two options of UFM1 transfer from UFC1 to the target. 1: directly to the substrate; 2: in a two-step mechanism, from UFC1 to UFL1 and then to the target.
Figure 3
Figure 3
Cellular targets of UFMylation and their cellular roles.
See this image and copyright information in PMC

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