DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells

Yinghao Zhang, Fang Mei Chang, Jianjun Huang, Jacob J. Junco, Shivani K. Maffi, Hannah I. Pridgen, Gabriel Catano, Hong Dang, Xiang Ding, Fuquan Yang, Dae Joon Kim, Thomas J. Slaga, Rongqiao He, Sung Jen Wei

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Timely removal of oxidatively damaged proteins is critical for cells exposed to oxidative stresses; however, cellular mechanism for clearing oxidized proteins is not clear. Our study reveals a novel type of protein modification that may play a role in targeting oxidized proteins and remove them. In this process, DSS1 (deleted in split hand/split foot 1), an evolutionally conserved small protein, is conjugated to proteins induced by oxidative stresses in vitro and in vivo, implying oxidized proteins are DSS1 clients. A subsequent ubiquitination targeting DSS1-protein adducts has been observed, suggesting the client proteins are degraded through the ubiquitin-proteasome pathway. The DSS1 attachment to its clients is evidenced to be an enzymatic process modulated by an unidentified ATPase. We name this novel protein modification as DSSylation, in which DSS1 plays as a modifier, whose attachment may render target proteins a signature leading to their subsequent ubiquitination, thereby recruits proteasome to degrade them.

Original languageEnglish (US)
Pages (from-to)124-140
Number of pages17
JournalProtein and Cell
Volume5
Issue number2
DOIs
StatePublished - Jan 1 2014

Keywords

  • DSS1
  • DSSylation
  • free radicals
  • oxidative stress
  • proteasome
  • protein modification
  • shfm1

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Drug Discovery
  • Cell Biology

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    Zhang, Y., Chang, F. M., Huang, J., Junco, J. J., Maffi, S. K., Pridgen, H. I., Catano, G., Dang, H., Ding, X., Yang, F., Kim, D. J., Slaga, T. J., He, R., & Wei, S. J. (2014). DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells. Protein and Cell, 5(2), 124-140. https://doi.org/10.1007/s13238-013-0018-8