Abstract
Here we performed studies to demonstrate SUMO4 maturation process. Unlike other SUMO proteins, cells under physiological condition mediate a rapid degradation for SUMO4. However, when cells under stressed condition, SUMO4 can be matured by the stress-induced endogenous hydrolase and be able to covalently conjugate to its substrate proteins. Furthermore, we failed to obtain evidence supporting a role for proline-90 unique to SUMO4 in its activation and functionality. Both wild-type SUMO4 and SUMO4-P90Q can be hydrolyzed by the stressed RAW264.7 cell lysates, and no significant functional difference between SUMO4, SUMO4-P90Q, and SUMO4-GG (matured form) was observed as determined by luciferase assay. However, the C-terminal di-glycine motif, a prerequisite for sumoylation, is necessary for SUMO4 to exert its functional activity. These data not only confirmed our previous published data, but also provided additional evidence suggesting a role for SUMO4 sumoylation in the regulation of intracellular stress.
Original language | English (US) |
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Pages (from-to) | 454-459 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 375 |
Issue number | 3 |
DOIs | |
State | Published - Oct 24 2008 |
Keywords
- Hydrolase
- Intracellular stress
- Maturation
- SUMO4
- Serum starvation
- Sumoylation
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology