Abstract
Our previous results showed that the polycomb protein mel-18 binds to a protein called HSF2 and inhibits HSF2 sumoylation, thereby functioning as an anti-SUMO E3 factor. This study also suggested that mel-18 regulates the sumoylation of other cellular proteins, but the identities of these other proteins were unknown. Here we show that mel-18 interacts with the RanGAP1 protein and inhibits its sumoylation, and that these activities do not require the RING domain of mel-18. The results also show that RanGAP1 sumoylation is decreased during mitosis, and that this is associated with increased interaction between RanGAP1 and mel-18 during this stage of the cell cycle. Intriguingly, this regulatory relationship is the opposite of that found for mel-18 and HSF2, in which the interaction between these two proteins decreases during mitosis, resulting in elevated HSF2 sumoylation. The results of this study strengthen the conclusion that mel-18 functions as an anti-SUMO E3 factor, and extend its targets to include regulation of the sumoylation of the important cellular protein RanGAP1.
Original language | English |
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Pages (from-to) | 252-255 |
Number of pages | 4 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 375 |
Issue number | 2 |
DOIs | |
State | Published - Oct 17 2008 |
Bibliographical note
Funding Information:We thank Mike Matunis for the RanGAP1 construct, and other members of the laboratory for insightful discussions. This research was supported by NIH Grant GM64606 to K.D.S.
Funding
We thank Mike Matunis for the RanGAP1 construct, and other members of the laboratory for insightful discussions. This research was supported by NIH Grant GM64606 to K.D.S.
Funders | Funder number |
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National Institutes of Health (NIH) | GM64606 |
National Institute of General Medical Sciences | R01GM061053 |
Keywords
- Mel-18
- Mitosis
- Polycomb
- RanGAP1
- SUMO
- SUMO-1
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology