RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation.
RAP80, a nuclear protein with two functional ubiquitin-interaction motifs (UIMs) at its N-terminus, plays a critical role in the regulation of estrogen receptor alpha and DNA damage response signaling. A yeast two-hybrid screen identified the SUMO-conjugating enzyme UBC9 as a protein interacting with RAP80. The interaction of RAP80 with UBC9 ... was confirmed by co-immunoprecipitation and GST pull-down analyses. The region between aa 122-204 was critical for the interaction of RAP80 with UBC9. In addition, we demonstrate that RAP80 is a target for SUMO-1 modification in intact cells. Expression of UBC9 enhanced RAP80 mono-sumoylation and also induced multi-sumoylation of RAP80. In addition to SUMO-1, RAP80 was efficiently conjugated to SUMO-3 but was only a weak substrate for SUMO-2 conjugation. These findings suggest that sumoylation plays a role in the regulation of RAP80 functions.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Carrier Proteins, DNA Damage, Estrogen Receptor alpha, Hela Cells, Humans, Molecular Sequence Data, Nuclear Proteins, Protein Structure, Tertiary, Radiation, Ionizing, SUMO-1 Protein, Signal Transduction, Two-Hybrid System Techniques, Ubiquitin, Ubiquitin-Conjugating Enzymes
Amino Acid Motifs, Amino Acid Sequence, Carrier Proteins, DNA Damage, Estrogen Receptor alpha, Hela Cells, Humans, Molecular Sequence Data, Nuclear Proteins, Protein Structure, Tertiary, Radiation, Ionizing, SUMO-1 Protein, Signal Transduction, Two-Hybrid System Techniques, Ubiquitin, Ubiquitin-Conjugating Enzymes
Biochem. Biophys. Res. Commun.
Date: Oct. 12, 2007
PubMed ID: 17698038
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