Drosophila peptidyl-prolyl isomerase Pin1 modulates circadian rhythms via regulating levels of PERIOD

So Who Kang; Euna Lee; Eunjoo Cho; Ji Hye Seo; Hyuk Wan Ko; Eun Young Kim

doi:10.1016/j.bbrc.2015.05.033

Drosophila peptidyl-prolyl isomerase Pin1 modulates circadian rhythms via regulating levels of PERIOD

So Who Kang, Euna Lee, Eunjoo Cho, Ji Hye Seo, Hyuk Wan Ko, Eun Young Kim

Department of Biochemistry

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

2 Citations (Scopus)

Abstract

In animal circadian clock machinery, the phosphorylation program of PERIOD (PER) leads to the spatio-temporal regulation of diverse PER functions, which are crucial for the maintenance of ∼24-hr circadian rhythmicity. The peptidyl-prolyl isomerase PIN1 modulates the diverse functions of its substrates by inducing conformational changes upon recognizing specific phosphorylated residues. Here, we show that overexpression of Drosophila pin1, dodo (dod), lengthens the locomotor behavioral period. Using Drosophila S2 cells, we demonstrate that Dod associates preferentially with phosphorylated species of PER, which delays the phosphorylation-dependent degradation of PER. Consistent with this, PER protein levels are higher in flies overexpressing dod. Taken together, we suggest that Dod plays a role in the maintenance of circadian period by regulating PER metabolism.

Original language	English
Pages (from-to)	235-240
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	463
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2015.05.033
Publication status	Published - 2015 Jun 14

Bibliographical note

Funding Information:
We thank the members of the EY Kim laboratory for critically reading this manuscript. This work was supported by the National Research Foundation of Korea (NRF) grant ( NRF-2014R1A2A1A11051765 , NRF-2012R1A5A2048183 ) funded by the Korean government and a 2011 grant to E.Y.K. from the Department of Medical Sciences funded by the graduate school of Ajou University.

Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Drosophila peptidyl-prolyl isomerase Pin1 modulates circadian rhythms via regulating levels of PERIOD",

abstract = "In animal circadian clock machinery, the phosphorylation program of PERIOD (PER) leads to the spatio-temporal regulation of diverse PER functions, which are crucial for the maintenance of ∼24-hr circadian rhythmicity. The peptidyl-prolyl isomerase PIN1 modulates the diverse functions of its substrates by inducing conformational changes upon recognizing specific phosphorylated residues. Here, we show that overexpression of Drosophila pin1, dodo (dod), lengthens the locomotor behavioral period. Using Drosophila S2 cells, we demonstrate that Dod associates preferentially with phosphorylated species of PER, which delays the phosphorylation-dependent degradation of PER. Consistent with this, PER protein levels are higher in flies overexpressing dod. Taken together, we suggest that Dod plays a role in the maintenance of circadian period by regulating PER metabolism.",

author = "Kang, {So Who} and Euna Lee and Eunjoo Cho and Seo, {Ji Hye} and Ko, {Hyuk Wan} and Kim, {Eun Young}",

note = "Funding Information: We thank the members of the EY Kim laboratory for critically reading this manuscript. This work was supported by the National Research Foundation of Korea (NRF) grant ( NRF-2014R1A2A1A11051765 , NRF-2012R1A5A2048183 ) funded by the Korean government and a 2011 grant to E.Y.K. from the Department of Medical Sciences funded by the graduate school of Ajou University. Publisher Copyright: {\textcopyright} 2015 Elsevier Inc. All rights reserved.",

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doi = "10.1016/j.bbrc.2015.05.033",

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AU - Kang, So Who

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AU - Cho, Eunjoo

AU - Seo, Ji Hye

AU - Ko, Hyuk Wan

AU - Kim, Eun Young

N1 - Funding Information: We thank the members of the EY Kim laboratory for critically reading this manuscript. This work was supported by the National Research Foundation of Korea (NRF) grant ( NRF-2014R1A2A1A11051765 , NRF-2012R1A5A2048183 ) funded by the Korean government and a 2011 grant to E.Y.K. from the Department of Medical Sciences funded by the graduate school of Ajou University. Publisher Copyright: © 2015 Elsevier Inc. All rights reserved.

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N2 - In animal circadian clock machinery, the phosphorylation program of PERIOD (PER) leads to the spatio-temporal regulation of diverse PER functions, which are crucial for the maintenance of ∼24-hr circadian rhythmicity. The peptidyl-prolyl isomerase PIN1 modulates the diverse functions of its substrates by inducing conformational changes upon recognizing specific phosphorylated residues. Here, we show that overexpression of Drosophila pin1, dodo (dod), lengthens the locomotor behavioral period. Using Drosophila S2 cells, we demonstrate that Dod associates preferentially with phosphorylated species of PER, which delays the phosphorylation-dependent degradation of PER. Consistent with this, PER protein levels are higher in flies overexpressing dod. Taken together, we suggest that Dod plays a role in the maintenance of circadian period by regulating PER metabolism.

AB - In animal circadian clock machinery, the phosphorylation program of PERIOD (PER) leads to the spatio-temporal regulation of diverse PER functions, which are crucial for the maintenance of ∼24-hr circadian rhythmicity. The peptidyl-prolyl isomerase PIN1 modulates the diverse functions of its substrates by inducing conformational changes upon recognizing specific phosphorylated residues. Here, we show that overexpression of Drosophila pin1, dodo (dod), lengthens the locomotor behavioral period. Using Drosophila S2 cells, we demonstrate that Dod associates preferentially with phosphorylated species of PER, which delays the phosphorylation-dependent degradation of PER. Consistent with this, PER protein levels are higher in flies overexpressing dod. Taken together, we suggest that Dod plays a role in the maintenance of circadian period by regulating PER metabolism.

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Drosophila peptidyl-prolyl isomerase Pin1 modulates circadian rhythms via regulating levels of PERIOD

Abstract

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