Mel-18 interacts with RanGAP1 and inhibits its sumoylation.
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.
Mesh Terms:
Cell Line, DNA-Binding Proteins, GTPase-Activating Proteins, Humans, RING Finger Domains, Repressor Proteins, Small Ubiquitin-Related Modifier Proteins, Ubiquitin-Conjugating Enzymes
Cell Line, DNA-Binding Proteins, GTPase-Activating Proteins, Humans, RING Finger Domains, Repressor Proteins, Small Ubiquitin-Related Modifier Proteins, Ubiquitin-Conjugating Enzymes
Biochem. Biophys. Res. Commun.
Date: Oct. 17, 2008
PubMed ID: 18706886
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