The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity

Byung Hak Ha, Kyung Hee Kim, Hee Min Yoo, Weontae Lee, Eunice EunKyeong Kim

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3 Citations (Scopus)


Ubiquitin-fold modifier 1 (Ufm1) specific protease (UfSP) is a novel cysteine protease that activates Ufm1 from its precursor by processing the C-terminus to expose the conserved Gly necessary for substrate conjugation and de-conjugates Ufm1 from the substrate. There are two forms: UfSP1 and UfSP2, the later with an additional domain at the N-terminus. Ufm1 and both the conjugating and deconjugating enzymes are highly conserved. However, in Caenorhabditis elegans there is one UfSP which has extra 136 residues at the N terminus compared to UfSP2. The crystal structure of cUfSP reveals that these additional residues display a MPN fold while the rest of the structure mimics that of UfSP2. The MPN domain does not have the metalloprotease activity found in some MPN-domain containing protein, rather it is required for the recognition and deufmylation of the substrate of cUfSP, UfBP1. In addition, the MPN domain is also required for localization to the endoplasmic reticulum.

Original languageEnglish
Pages (from-to)450-456
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 2016 Aug 5

Bibliographical note

Funding Information:
We thank the staff at 4A beamline, Pohang Accelerator Laboratory, Korea. This work was supported by grant from the Global Research Laboratory program of the Ministry of Science, ICT and Future Planning of Korea (MISP: grant No. NRF 20110021713 ), and grant from Korea Institute of Science and Technology ( 2E26360 ).

Publisher Copyright:
© 2016 Elsevier Inc.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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