Decrypting UFMylation: How proteins are modified with UFM1

Sayanika Banerjee, Manoj Kumar, Reuven Wiener*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

30 Scopus citations

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.

Original languageAmerican English
Article number1442
Pages (from-to)1-14
Number of pages14
JournalBiomolecules
Volume10
Issue number10
DOIs
StatePublished - Oct 2020

Bibliographical note

Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Keywords

  • Conjugating enzymes
  • UBA5
  • UFC1
  • UFL1
  • UFM1
  • UFMylation
  • Ubiquitin-like proteins

Fingerprint

Dive into the research topics of 'Decrypting UFMylation: How proteins are modified with UFM1'. Together they form a unique fingerprint.

Cite this