{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["4(1)"],"submitter":["Wang L"],"pubmed_abstract":["The plant UV-B photoreceptor UV RESISTANCE LOCUS 8 (UVR8) exists as a homodimer in its inactive ground state. Upon UV-B exposure, UVR8 monomerizes and interacts with a downstream key regulator, the CONSTITUTIVE PHOTOMORPHOGENIC 1/SUPPRESSOR OF PHYA (COP1/SPA) E3 ubiquitin ligase complex, to initiate UV-B signaling. Two WD40 proteins, REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1 (RUP1) and RUP2 directly interact with monomeric UVR8 and facilitate UVR8 ground state reversion, completing the UVR8 photocycle. Here, we reconstituted the RUP-mediated UVR8 redimerization process in vitro and reported the structure of the RUP2-UVR8<sup>W285A</sup> complex (2.0 Å). RUP2 and UVR8<sup>W285A</sup> formed a heterodimer via two distinct interfaces, designated Interface 1 and 2. The previously characterized In"],"journal":["Plant communications"],"pagination":["100428"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9860181"],"repository":["biostudies-literature"],"pubmed_title":["RUP2 facilitates UVR8 redimerization via two interfaces."],"pmcid":["PMC9860181"],"pubmed_authors":["Yan J","Zhang D","Ma L","Wang L","Qiu L","Ren H","Wen J","Guan Z","Huang X","Yin P","Wang Y","Chang H","Wu X"],"additional_accession":[]},"is_claimable":false,"name":"RUP2 facilitates UVR8 redimerization via two interfaces.","description":"The plant UV-B photoreceptor UV RESISTANCE LOCUS 8 (UVR8) exists as a homodimer in its inactive ground state. Upon UV-B exposure, UVR8 monomerizes and interacts with a downstream key regulator, the CONSTITUTIVE PHOTOMORPHOGENIC 1/SUPPRESSOR OF PHYA (COP1/SPA) E3 ubiquitin ligase complex, to initiate UV-B signaling. Two WD40 proteins, REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1 (RUP1) and RUP2 directly interact with monomeric UVR8 and facilitate UVR8 ground state reversion, completing the UVR8 photocycle. Here, we reconstituted the RUP-mediated UVR8 redimerization process in vitro and reported the structure of the RUP2-UVR8<sup>W285A</sup> complex (2.0 Å). RUP2 and UVR8<sup>W285A</sup> formed a heterodimer via two distinct interfaces, designated Interface 1 and 2. The previously characterized In","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-28T16:45:32.102Z","creation":"2024-11-19T19:09:19.14Z"},"accession":"S-EPMC9860181","cross_references":{"pubmed":["36065466"],"doi":["10.1016/j.xplc.2022.100428"]}}