Ultraviolet-B-mediated induction of protein–protein interactions in mammalian cells

Crefcoeur, Remco Paul; Yin, Ruohe; Ulm, Roman; Halazonetis, Thanos D.

doi:10.1038/ncomms2800

Cited by 128 publications

(131 citation statements)

References 19 publications

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“…The specificity and sensitivity of UVR8 to UV-B indicate that it will be a promising addition to the optogenetic toolkit, allowing UV-B to exert regulation in a visible light background. Indeed, first implementations of UVR8 in novel optogenetic systems were recently reported whereby UV-B was used to control nuclear retention, chromatin association, protein secretion and gene expression in mammalian cells (Chen et al 2013, Crefcoeur et al 2013. In agriculture, our increasing knowledge of UV-B protective mechanisms employed by the plant may potentially lead to industrial applications.…”

Section: Discussionmentioning

confidence: 99%

The UVR8 UV-B Photoreceptor: Perception, Signaling and Response

Tilbrook

Arongaus

Binkert

et al. 2013

The Arabidopsis Book

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224

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Ultraviolet-B radiation (UV-B)is an intrinsic part of sunlight that is accompanied by significant biological effects. Plants are able to perceive UV-B using the UV-B photoreceptor UVR8 which is linked to a specific molecular signaling pathway and leads to UV-B acclimation. Herein we review the biological process in plants from initial UV-B perception and signal transduction through to the known UV-B responses that promote survival in sunlight. The UVR8 UV-B photoreceptor exists as a homodimer that instantly monomerises upon UV-B absorption via specific intrinsic tryptophans which act as UV-B chromophores. The UVR8 monomer interacts with COP1, an E3 ubiquitin ligase, initiating a molecular signaling pathway that leads to gene expression changes. This signaling output leads to UVR8-dependent responses including UV-B-induced photomorphogenesis and the accumulation of UV-B-absorbing flavonols. Negative feedback regulation of the pathway is provided by the WD40-repeat proteins RUP1 and RUP2, which facilitate UVR8 redimerization, disrupting the UVR8-COP1 interaction. Despite rapid advancements in the field of recent years, further components of UVR8 UV-B signaling are constantly emerging, and the precise interplay of these and the established players UVR8, COP1, RUP1, RUP2 and HY5 needs to be defined. UVR8 UV-B signaling represents our further understanding of how plants are able to sense their light environment and adjust their growth accordingly.

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Section: Discussionmentioning

confidence: 99%

The UVR8 UV-B Photoreceptor: Perception, Signaling and Response

Tilbrook

Arongaus

Binkert

et al. 2013

The Arabidopsis Book

Self Cite

224

187

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“…Yeast growth assays to detect colonies with interacting proteins were performed at 30°C on selective SD/-Trp/-Leu/-His medium. The quantitative interaction assays were performed using chlorophenol red-b-D-galactopyranoside (Roche Applied Science) as the substrate as described previously (Rizzini et al, 2011;Crefcoeur et al, 2013). For the yeast twohybrid assays with UVR8 DC27 and COP1, UVR8 DC27 was cloned in-frame to the Gal4 DNA binding domain in pGBKT7-GW, and COP1 was used in the pGADT7-GW vector.…”

Section: Protein Extraction Immunoprecipitation and Immunoblotsmentioning

confidence: 99%

“…If needed, irradiation of yeast cells by narrow-band UV-B (Philips TL20W/01RS; 20 h, 1.5 mmol m 22 s 21 ) was performed as described previously (Rizzini et al, 2011;Crefcoeur et al, 2013).…”

Section: Protein Extraction Immunoprecipitation and Immunoblotsmentioning

confidence: 99%

Two Distinct Domains of the UVR8 Photoreceptor Interact with COP1 to Initiate UV-B Signaling in Arabidopsis

et al. 2015

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UV-B photon reception by the Arabidopsis thaliana homodimeric UV RESISTANCE LOCUS8 (UVR8) photoreceptor leads to its monomerization and a crucial interaction with CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1). Relay of the subsequent signal regulates UV-B-induced photomorphogenesis and stress acclimation. Here, we report that two separate domains of UVR8 interact with COP1: the b-propeller domain of UVR8 mediates UV-B-dependent interaction with the WD40 repeats-based predicted b-propeller domain of COP1, whereas COP1 activity is regulated by interaction through the UVR8 C-terminal C27 domain. We show not only that the C27 domain is required for UVR8 activity but also that chemically induced expression of the C27 domain is sufficient to mimic UV-B signaling. We further show, in contrast with COP1, that the WD40 repeat proteins REPRESSOR OF UV-B PHOTOMORPHOGENESIS1 (RUP1) and RUP2 interact only with the UVR8 C27 domain. This coincides with their facilitation of UVR8 reversion to the ground state by redimerization and their potential to interact with UVR8 in a UV-B-independent manner. Collectively, our results provide insight into a key mechanism of photoreceptor-mediated signaling and its negative feedback regulation.

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“…In recent years a wide spectrum of aspects related to UVR8 function has been addressed in the literature (15,16). Still, the mechanism that links UV-B absorption to the dissociation of the photoreceptor remains unclear.…”

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confidence: 99%

On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor

Voityuk

Marcus

Michel‐Beyerle

2014

Proc. Natl. Acad. Sci. U.S.A.

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UV-B absorption by the photoreceptor UV resistance locus 8 (UVR8) consisting of two identical protein units triggers a signal chain used by plants in connection with protection and repair of UV-B induced damage. X-ray structural analysis of the purified protein [Christie JM, et al. (2012) Science 335(6075):1492-1496] [Wu D, et al. (2012) Nature 484(7393): 214-220] has revealed that the dimer is held together by arginine-aspartate salt bridges. In this paper we address the initial processes in the signal chain. On the basis of high-level quantum-chemical calculations, we propose a mechanism for the photodissociation of UVR8 that consists of three steps: (i) In each monomer, multiple tryptophans form an extended light-harvesting system in which the L a excited state of Trp233 experiences strong electrostatic stabilization by the protein environment. The strong stabilization singles out this tryptophan to be an efficient exciton acceptor that accumulates the excitation energy from the entire protein subunit. (ii) A fast decay of the locally excited state by charge separation generates the radical ion pair Trp285(+)-Trp233(−) with a dipole moment of ∼18 D. (iii) Key to the proposed mechanism is that this large dipole moment drives the breaking of the salt bridges between the two monomer subunits. The suggested mechanism for the UV-B-driven dissociation of the dimer that rests on the prominent players Trp233 and Trp285 explains the experimental results obtained from mutagenesis of UVR8. L ife on earth depends on sunlight that drives energy conversion and signaling processes, however, at the price that its UV fraction may damage DNA. Counteracting this threat, plants respond to UV-B radiation by the photoreceptor UV resistance locus 8 (UVR8) discovered in Arabidopsis thaliana (1). In the presence of UV-B (280-315 nm), the UVR8 protein accumulates rapidly in the cell nucleus (2, 3). Its interaction with other proteins activates gene expression to protect against or repair UV-B-induced damage (4-7). Unlike other photoreceptors in cells, the protein UVR8 exploits the UV-B absorbance of its intrinsic tryptophans rather than that of exogenic chromophores.The crystal structure of the UVR8 protein (8, 9) revealed that the dimer is held together by salt bridges between the cationic arginine (R) and anionic aspartate (D) or glutamate (E) side chains at the interface between the two subunits. Exposure of UVR8 to UV-B light causes dissociation of the protein into the monomers. This monomerization is universal, because it is observed for the purified protein (8, 9) and in plants and heterologous systems (10). The crystal structure allows one to infer a cooperative role and an interplay of specific tryptophans. It was suggested (11, 12) that excitation of the tryptophan triad W233, W285, and W337 initiates the dissociation of the dimeric photoreceptor and triggers the signal chain used by plants for . Subsequent interactions of monomer subunits with other proteins associated with chromatin have been shown to activate transcription...

show abstract

Ultraviolet-B-mediated induction of protein–protein interactions in mammalian cells

Cited by 128 publications

References 19 publications

The UVR8 UV-B Photoreceptor: Perception, Signaling and Response

The UVR8 UV-B Photoreceptor: Perception, Signaling and Response

Two Distinct Domains of the UVR8 Photoreceptor Interact with COP1 to Initiate UV-B Signaling in Arabidopsis

On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor

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