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RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation.

ABSTRACT: 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.

SUBMITTER: Yan J

PROVIDER: S-EPMC2049087 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation.

Yan Jun J Yang Xiao-Ping XP Kim Yong-Sik YS Joo Joung Hyuck JH Jetten Anton M AM

Biochemical and biophysical research communications 20070808 1

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 ad ...[more]

PMID: 17698038

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