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Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1)
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| Zeitschriftentitel: | Genes & Development |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Genes & Development, 21, 2007, 12, S. 1506-1518 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita |
|---|---|
| author |
Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita |
| spellingShingle |
Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita Genes & Development Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) Developmental Biology Genetics |
| author_sort |
fang, yanshan |
| spelling |
Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1541607 <jats:p>Phosphorylation is an important timekeeping mechanism in the circadian clock that has been closely studied at the level of the kinases involved but may also be tightly controlled by phosphatase action. Here we demonstrate a role for protein phosphatase 1 (PP1) in the regulation of the major timekeeping molecules in the <jats:italic>Drosophila</jats:italic> clock, TIMELESS (TIM) and PERIOD (PER). Flies with reduced PP1 activity exhibit a lengthened circadian period, reduced amplitude of behavioral rhythms, and an altered response to light that suggests a defect in the rising phase of clock protein expression. On a molecular level, PP1 directly dephosphorylates TIM and stabilizes it in both S2R<jats:sup>+</jats:sup> cells and clock neurons. However, PP1 does not act in a simple antagonistic manner to SHAGGY (SGG), the kinase that phosphorylates TIM, because the behavioral phenotypes produced by inhibiting PP1 in flies are different from those achieved by overexpressing SGG. PP1 also acts on PER, and TIM regulates the control of PER by PP1, although it does not affect PP2A action on PER. We propose a modified model for post-translational regulation of the <jats:italic>Drosophila</jats:italic> clock, in which PP1 is critical for the rhythmic abundance of TIM/PER while PP2A also regulates the nuclear translocation of TIM/PER.</jats:p> Post-translational regulation of the <i>Drosophila</i> circadian clock requires protein phosphatase 1 (PP1) Genes & Development |
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| title |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_unstemmed |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_full |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_fullStr |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_full_unstemmed |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_short |
Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_sort |
post-translational regulation of the <i>drosophila</i> circadian clock requires protein phosphatase 1 (pp1) |
| topic |
Developmental Biology Genetics |
| url |
http://dx.doi.org/10.1101/gad.1541607 |
| publishDate |
2007 |
| physical |
1506-1518 |
| description |
<jats:p>Phosphorylation is an important timekeeping mechanism in the circadian clock that has been closely studied at the level of the kinases involved but may also be tightly controlled by phosphatase action. Here we demonstrate a role for protein phosphatase 1 (PP1) in the regulation of the major timekeeping molecules in the <jats:italic>Drosophila</jats:italic> clock, TIMELESS (TIM) and PERIOD (PER). Flies with reduced PP1 activity exhibit a lengthened circadian period, reduced amplitude of behavioral rhythms, and an altered response to light that suggests a defect in the rising phase of clock protein expression. On a molecular level, PP1 directly dephosphorylates TIM and stabilizes it in both S2R<jats:sup>+</jats:sup> cells and clock neurons. However, PP1 does not act in a simple antagonistic manner to SHAGGY (SGG), the kinase that phosphorylates TIM, because the behavioral phenotypes produced by inhibiting PP1 in flies are different from those achieved by overexpressing SGG. PP1 also acts on PER, and TIM regulates the control of PER by PP1, although it does not affect PP2A action on PER. We propose a modified model for post-translational regulation of the <jats:italic>Drosophila</jats:italic> clock, in which PP1 is critical for the rhythmic abundance of TIM/PER while PP2A also regulates the nuclear translocation of TIM/PER.</jats:p> |
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| author | Fang, Yanshan, Sathyanarayanan, Sriram, Sehgal, Amita |
| author_facet | Fang, Yanshan, Sathyanarayanan, Sriram, Sehgal, Amita, Fang, Yanshan, Sathyanarayanan, Sriram, Sehgal, Amita |
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| description | <jats:p>Phosphorylation is an important timekeeping mechanism in the circadian clock that has been closely studied at the level of the kinases involved but may also be tightly controlled by phosphatase action. Here we demonstrate a role for protein phosphatase 1 (PP1) in the regulation of the major timekeeping molecules in the <jats:italic>Drosophila</jats:italic> clock, TIMELESS (TIM) and PERIOD (PER). Flies with reduced PP1 activity exhibit a lengthened circadian period, reduced amplitude of behavioral rhythms, and an altered response to light that suggests a defect in the rising phase of clock protein expression. On a molecular level, PP1 directly dephosphorylates TIM and stabilizes it in both S2R<jats:sup>+</jats:sup> cells and clock neurons. However, PP1 does not act in a simple antagonistic manner to SHAGGY (SGG), the kinase that phosphorylates TIM, because the behavioral phenotypes produced by inhibiting PP1 in flies are different from those achieved by overexpressing SGG. PP1 also acts on PER, and TIM regulates the control of PER by PP1, although it does not affect PP2A action on PER. We propose a modified model for post-translational regulation of the <jats:italic>Drosophila</jats:italic> clock, in which PP1 is critical for the rhythmic abundance of TIM/PER while PP2A also regulates the nuclear translocation of TIM/PER.</jats:p> |
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| imprint | Cold Spring Harbor Laboratory, 2007 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2007 |
| institution | DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3 |
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| spelling | Fang, Yanshan Sathyanarayanan, Sriram Sehgal, Amita 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1541607 <jats:p>Phosphorylation is an important timekeeping mechanism in the circadian clock that has been closely studied at the level of the kinases involved but may also be tightly controlled by phosphatase action. Here we demonstrate a role for protein phosphatase 1 (PP1) in the regulation of the major timekeeping molecules in the <jats:italic>Drosophila</jats:italic> clock, TIMELESS (TIM) and PERIOD (PER). Flies with reduced PP1 activity exhibit a lengthened circadian period, reduced amplitude of behavioral rhythms, and an altered response to light that suggests a defect in the rising phase of clock protein expression. On a molecular level, PP1 directly dephosphorylates TIM and stabilizes it in both S2R<jats:sup>+</jats:sup> cells and clock neurons. However, PP1 does not act in a simple antagonistic manner to SHAGGY (SGG), the kinase that phosphorylates TIM, because the behavioral phenotypes produced by inhibiting PP1 in flies are different from those achieved by overexpressing SGG. PP1 also acts on PER, and TIM regulates the control of PER by PP1, although it does not affect PP2A action on PER. We propose a modified model for post-translational regulation of the <jats:italic>Drosophila</jats:italic> clock, in which PP1 is critical for the rhythmic abundance of TIM/PER while PP2A also regulates the nuclear translocation of TIM/PER.</jats:p> Post-translational regulation of the <i>Drosophila</i> circadian clock requires protein phosphatase 1 (PP1) Genes & Development |
| spellingShingle | Fang, Yanshan, Sathyanarayanan, Sriram, Sehgal, Amita, Genes & Development, Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1), Developmental Biology, Genetics |
| title | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_full | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_fullStr | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_full_unstemmed | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_short | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| title_sort | post-translational regulation of the <i>drosophila</i> circadian clock requires protein phosphatase 1 (pp1) |
| title_unstemmed | Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1) |
| topic | Developmental Biology, Genetics |
| url | http://dx.doi.org/10.1101/gad.1541607 |