Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.

Throughout the day, clock proteins synchronize changes in animal physiology (e.g., wakefulness and appetite) with external cues (e.g., daylight and food). In vertebrates, both casein kinase 1 delta and epsilon (CK1δ and CK1ε) regulate these circadian changes by phosphorylating other core clock prote...

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Autores principales:	Lorna S Kategaya, Aisha Hilliard, Louying Zhang, John M Asara, Louis J Ptáček, Ying-Hui Fu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/76d47a1603a3459389664b2b7efe0113
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id	oai:doaj.org-article:76d47a1603a3459389664b2b7efe0113
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spelling	oai:doaj.org-article:76d47a1603a3459389664b2b7efe01132021-11-18T07:26:41ZCasein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.1932-620310.1371/journal.pone.0031987https://doaj.org/article/76d47a1603a3459389664b2b7efe01132012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22384121/?tool=EBIhttps://doaj.org/toc/1932-6203Throughout the day, clock proteins synchronize changes in animal physiology (e.g., wakefulness and appetite) with external cues (e.g., daylight and food). In vertebrates, both casein kinase 1 delta and epsilon (CK1δ and CK1ε) regulate these circadian changes by phosphorylating other core clock proteins. In addition, CK1 can regulate circadian-dependent transcription in a non-catalytic manner, however, the mechanism is unknown. Furthermore, the extent of functional redundancy between these closely related kinases is debated. To further advance knowledge about CK1δ and CK1ε mechanisms of action in the biological clock, we first carried out proteomic analysis of both kinases in human cells. Next, we tested interesting candidates in a cell-based circadian readout which resulted in the discovery of PROHIBITIN 2 (PHB2) as a modulator of period length. Decreasing the expression of PHB2 increases circadian-driven transcription, thus revealing PHB2 acts as an inhibitor in the molecular clock. While stable binding of PHB2 to either kinase was not detected, knocking down CK1ε expression increases PHB2 protein levels and, unexpectedly, knocking down CK1δ decreases PHB2 transcript levels. Thus, isolating CK1 protein complexes led to the identification of PHB2 as an inhibitor of circadian transcription. Furthermore, we show that CK1δ and CK1ε differentially regulate the expression of PHB2.Lorna S KategayaAisha HilliardLouying ZhangJohn M AsaraLouis J PtáčekYing-Hui FuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e31987 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lorna S Kategaya Aisha Hilliard Louying Zhang John M Asara Louis J Ptáček Ying-Hui Fu Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
description	Throughout the day, clock proteins synchronize changes in animal physiology (e.g., wakefulness and appetite) with external cues (e.g., daylight and food). In vertebrates, both casein kinase 1 delta and epsilon (CK1δ and CK1ε) regulate these circadian changes by phosphorylating other core clock proteins. In addition, CK1 can regulate circadian-dependent transcription in a non-catalytic manner, however, the mechanism is unknown. Furthermore, the extent of functional redundancy between these closely related kinases is debated. To further advance knowledge about CK1δ and CK1ε mechanisms of action in the biological clock, we first carried out proteomic analysis of both kinases in human cells. Next, we tested interesting candidates in a cell-based circadian readout which resulted in the discovery of PROHIBITIN 2 (PHB2) as a modulator of period length. Decreasing the expression of PHB2 increases circadian-driven transcription, thus revealing PHB2 acts as an inhibitor in the molecular clock. While stable binding of PHB2 to either kinase was not detected, knocking down CK1ε expression increases PHB2 protein levels and, unexpectedly, knocking down CK1δ decreases PHB2 transcript levels. Thus, isolating CK1 protein complexes led to the identification of PHB2 as an inhibitor of circadian transcription. Furthermore, we show that CK1δ and CK1ε differentially regulate the expression of PHB2.
format	article
author	Lorna S Kategaya Aisha Hilliard Louying Zhang John M Asara Louis J Ptáček Ying-Hui Fu
author_facet	Lorna S Kategaya Aisha Hilliard Louying Zhang John M Asara Louis J Ptáček Ying-Hui Fu
author_sort	Lorna S Kategaya
title	Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
title_short	Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
title_full	Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
title_fullStr	Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
title_full_unstemmed	Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
title_sort	casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/76d47a1603a3459389664b2b7efe0113
work_keys_str_mv	AT lornaskategaya caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock AT aishahilliard caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock AT louyingzhang caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock AT johnmasara caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock AT louisjptacek caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock AT yinghuifu caseinkinase1proteomicsrevealprohibitin2functioninmolecularclock
_version_	1718423416387665920

Casein kinase 1 proteomics reveal prohibitin 2 function in molecular clock.

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