Format

Send to

Choose Destination
Protein Cell. 2014 Feb;5(2):124-40. doi: 10.1007/s13238-013-0018-8. Epub 2014 Feb 11.

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

Author information

1
Medical Research Division, Regional Academic Health Center, Edinburg, TX, 78541, USA.

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.

PMID:
24515614
PMCID:
PMC3956975
DOI:
10.1007/s13238-013-0018-8
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Springer Icon for PubMed Central
Loading ...
Support Center