Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer

Jong Sang Ryu; Jeong Il Kim; Tim Kunkel; Byung Chul Kim; Dae Shik Cho; Sung Hyun Hong; Seong Hee Kim; Aurora Piñas Fernández; Yumi Kim; Jose M. Alonso; Joseph R. Ecker; Ferenc Nagy; Pyung Ok Lim; Pill Soon Song; Eberhard Schäfer; Hong Gil Nam

doi:10.1016/j.cell.2004.12.019

Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer

Jong Sang Ryu, Jeong Il Kim, Tim Kunkel, Byung Chul Kim, Dae Shik Cho, Sung Hyun Hong, Seong Hee Kim, Aurora Piñas Fernández, Yumi Kim, Jose M. Alonso, Joseph R. Ecker, Ferenc Nagy, Pyung Ok Lim, Pill Soon Song, Eberhard Schäfer, Hong Gil Nam

Department of New Biology

Research output: Contribution to journal › Article › peer-review

139 Scopus citations

Abstract

Environmental light information such as quality, intensity, and duration in red (∼660 nm) and far-red (∼730 nm) wavelengths is perceived by phytochrome photoreceptors in plants, critically influencing almost all developmental strategies from germination to flowering. Phytochromes interconvert between red light-absorbing Pr and biologically functional far-red light-absorbing Pfr forms. To ensure optimal photoresponses in plants, the flux of light signal from Pfr-phytochromes should be tightly controlled. Phytochromes are phosphorylated at specific serine residues. We found that a type 5 protein phosphatase (PAPP5) specifically dephosphorylates biologically active Pfr-phytochromes and enhances phytochrome-mediated photoresponses. Depending on the specific serine residues dephosphorylated by PAPP5, phytochrome stability and affinity for a downstream signal transducer, NDPK2, were enhanced. Thus, phytochrome photoreceptors have developed an elaborate biochemical tuning mechanism for modulating the flux of light signal, employing variable phosphorylation states controlled by phosphorylation and PAPP5-mediated dephosphorylation as a mean to control phytochrome stability and affinity for downstream transducers.

Original language	English
Pages (from-to)	395-406
Number of pages	12
Journal	Cell
Volume	120
Issue number	3
DOIs	https://doi.org/10.1016/j.cell.2004.12.019
State	Published - 11 Feb 2005

Bibliographical note

Funding Information:
We thank Dr. Joanne Chory for providing the Arabidopsis PHYA and PHYB cDNAs and Diana Bauer for help with confocal microscopy. This research was supported by grants from the Crop Functional Genomics Frontier Research Program (to H.G.N; CG1311), in part from the BioGreen 21 program of Rural Development Administration (to P.-S.S.), in part from the Environmental Biotechnology National Core Research Center program of KOSEF/MOST (to J.-I.K. and P.-S.S; R15-2003-012-01003-0).

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Ryu, J. S., Kim, J. I., Kunkel, T., Kim, B. C., Cho, D. S., Hong, S. H., Kim, S. H., Fernández, A. P., Kim, Y., Alonso, J. M., Ecker, J. R., Nagy, F., Lim, P. O., Song, P. S., Schäfer, E., & Nam, H. G. (2005). Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer. Cell, 120(3), 395-406. https://doi.org/10.1016/j.cell.2004.12.019

@article{cc67c8a58df4431883c0b2954f8c6fd3,

title = "Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer",

abstract = "Environmental light information such as quality, intensity, and duration in red (∼660 nm) and far-red (∼730 nm) wavelengths is perceived by phytochrome photoreceptors in plants, critically influencing almost all developmental strategies from germination to flowering. Phytochromes interconvert between red light-absorbing Pr and biologically functional far-red light-absorbing Pfr forms. To ensure optimal photoresponses in plants, the flux of light signal from Pfr-phytochromes should be tightly controlled. Phytochromes are phosphorylated at specific serine residues. We found that a type 5 protein phosphatase (PAPP5) specifically dephosphorylates biologically active Pfr-phytochromes and enhances phytochrome-mediated photoresponses. Depending on the specific serine residues dephosphorylated by PAPP5, phytochrome stability and affinity for a downstream signal transducer, NDPK2, were enhanced. Thus, phytochrome photoreceptors have developed an elaborate biochemical tuning mechanism for modulating the flux of light signal, employing variable phosphorylation states controlled by phosphorylation and PAPP5-mediated dephosphorylation as a mean to control phytochrome stability and affinity for downstream transducers.",

author = "Ryu, {Jong Sang} and Kim, {Jeong Il} and Tim Kunkel and Kim, {Byung Chul} and Cho, {Dae Shik} and Hong, {Sung Hyun} and Kim, {Seong Hee} and Fern{\'a}ndez, {Aurora Pi{\~n}as} and Yumi Kim and Alonso, {Jose M.} and Ecker, {Joseph R.} and Ferenc Nagy and Lim, {Pyung Ok} and Song, {Pill Soon} and Eberhard Sch{\"a}fer and Nam, {Hong Gil}",

note = "Funding Information: We thank Dr. Joanne Chory for providing the Arabidopsis PHYA and PHYB cDNAs and Diana Bauer for help with confocal microscopy. This research was supported by grants from the Crop Functional Genomics Frontier Research Program (to H.G.N; CG1311), in part from the BioGreen 21 program of Rural Development Administration (to P.-S.S.), in part from the Environmental Biotechnology National Core Research Center program of KOSEF/MOST (to J.-I.K. and P.-S.S; R15-2003-012-01003-0). ",

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doi = "10.1016/j.cell.2004.12.019",

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Ryu, JS, Kim, JI, Kunkel, T, Kim, BC, Cho, DS, Hong, SH, Kim, SH, Fernández, AP, Kim, Y, Alonso, JM, Ecker, JR, Nagy, F, Lim, PO, Song, PS, Schäfer, E & Nam, HG 2005, 'Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer', Cell, vol. 120, no. 3, pp. 395-406. https://doi.org/10.1016/j.cell.2004.12.019

TY - JOUR

T1 - Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer

AU - Ryu, Jong Sang

AU - Kim, Jeong Il

AU - Kunkel, Tim

AU - Kim, Byung Chul

AU - Cho, Dae Shik

AU - Hong, Sung Hyun

AU - Kim, Seong Hee

AU - Fernández, Aurora Piñas

AU - Kim, Yumi

AU - Alonso, Jose M.

AU - Ecker, Joseph R.

AU - Nagy, Ferenc

AU - Lim, Pyung Ok

AU - Song, Pill Soon

AU - Schäfer, Eberhard

AU - Nam, Hong Gil

N1 - Funding Information: We thank Dr. Joanne Chory for providing the Arabidopsis PHYA and PHYB cDNAs and Diana Bauer for help with confocal microscopy. This research was supported by grants from the Crop Functional Genomics Frontier Research Program (to H.G.N; CG1311), in part from the BioGreen 21 program of Rural Development Administration (to P.-S.S.), in part from the Environmental Biotechnology National Core Research Center program of KOSEF/MOST (to J.-I.K. and P.-S.S; R15-2003-012-01003-0).

PY - 2005/2/11

Y1 - 2005/2/11

N2 - Environmental light information such as quality, intensity, and duration in red (∼660 nm) and far-red (∼730 nm) wavelengths is perceived by phytochrome photoreceptors in plants, critically influencing almost all developmental strategies from germination to flowering. Phytochromes interconvert between red light-absorbing Pr and biologically functional far-red light-absorbing Pfr forms. To ensure optimal photoresponses in plants, the flux of light signal from Pfr-phytochromes should be tightly controlled. Phytochromes are phosphorylated at specific serine residues. We found that a type 5 protein phosphatase (PAPP5) specifically dephosphorylates biologically active Pfr-phytochromes and enhances phytochrome-mediated photoresponses. Depending on the specific serine residues dephosphorylated by PAPP5, phytochrome stability and affinity for a downstream signal transducer, NDPK2, were enhanced. Thus, phytochrome photoreceptors have developed an elaborate biochemical tuning mechanism for modulating the flux of light signal, employing variable phosphorylation states controlled by phosphorylation and PAPP5-mediated dephosphorylation as a mean to control phytochrome stability and affinity for downstream transducers.

AB - Environmental light information such as quality, intensity, and duration in red (∼660 nm) and far-red (∼730 nm) wavelengths is perceived by phytochrome photoreceptors in plants, critically influencing almost all developmental strategies from germination to flowering. Phytochromes interconvert between red light-absorbing Pr and biologically functional far-red light-absorbing Pfr forms. To ensure optimal photoresponses in plants, the flux of light signal from Pfr-phytochromes should be tightly controlled. Phytochromes are phosphorylated at specific serine residues. We found that a type 5 protein phosphatase (PAPP5) specifically dephosphorylates biologically active Pfr-phytochromes and enhances phytochrome-mediated photoresponses. Depending on the specific serine residues dephosphorylated by PAPP5, phytochrome stability and affinity for a downstream signal transducer, NDPK2, were enhanced. Thus, phytochrome photoreceptors have developed an elaborate biochemical tuning mechanism for modulating the flux of light signal, employing variable phosphorylation states controlled by phosphorylation and PAPP5-mediated dephosphorylation as a mean to control phytochrome stability and affinity for downstream transducers.

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U2 - 10.1016/j.cell.2004.12.019

DO - 10.1016/j.cell.2004.12.019

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C2 - 15707897

AN - SCOPUS:13544255502

SN - 0092-8674

VL - 120

SP - 395

EP - 406

JO - Cell

JF - Cell

IS - 3

ER -

Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer

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