Activating PER repressor through a DBT-directed phosphorylation switch.

Protein phosphorylation plays an essential role in the generation of circadian rhythms, regulating the stability, activity, and subcellular localization of certain proteins that constitute the biological clock. This study examines the role of the protein kinase Doubletime (DBT), a Drosophila ortholo...

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Autores principales:	Saul Kivimäe, Lino Saez, Michael W Young
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/26dd9adf4af44767ba443cacc77cf066
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spelling	oai:doaj.org-article:26dd9adf4af44767ba443cacc77cf0662021-11-25T05:33:15ZActivating PER repressor through a DBT-directed phosphorylation switch.1544-91731545-788510.1371/journal.pbio.0060183https://doaj.org/article/26dd9adf4af44767ba443cacc77cf0662008-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18666831/pdf/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Protein phosphorylation plays an essential role in the generation of circadian rhythms, regulating the stability, activity, and subcellular localization of certain proteins that constitute the biological clock. This study examines the role of the protein kinase Doubletime (DBT), a Drosophila ortholog of human casein kinase I (CKI)epsilon/delta. An enzymatically active DBT protein is shown to directly phosphorylate the Drosophila clock protein Period (PER). DBT-dependent phosphorylation sites are identified within PER, and their functional significance is assessed in a cultured cell system and in vivo. The per(S) mutation, which is associated with short-period (19-h) circadian rhythms, alters a key phosphorylation target within PER. Inspection of this and neighboring sequence variants indicates that several DBT-directed phosphorylations regulate PER activity in an integrated fashion: Alternative phosphorylations of two adjoining sequence motifs appear to be associated with switch-like changes in PER stability and repressor function.Saul KivimäeLino SaezMichael W YoungPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 6, Iss 7, p e183 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Saul Kivimäe Lino Saez Michael W Young Activating PER repressor through a DBT-directed phosphorylation switch.
description	Protein phosphorylation plays an essential role in the generation of circadian rhythms, regulating the stability, activity, and subcellular localization of certain proteins that constitute the biological clock. This study examines the role of the protein kinase Doubletime (DBT), a Drosophila ortholog of human casein kinase I (CKI)epsilon/delta. An enzymatically active DBT protein is shown to directly phosphorylate the Drosophila clock protein Period (PER). DBT-dependent phosphorylation sites are identified within PER, and their functional significance is assessed in a cultured cell system and in vivo. The per(S) mutation, which is associated with short-period (19-h) circadian rhythms, alters a key phosphorylation target within PER. Inspection of this and neighboring sequence variants indicates that several DBT-directed phosphorylations regulate PER activity in an integrated fashion: Alternative phosphorylations of two adjoining sequence motifs appear to be associated with switch-like changes in PER stability and repressor function.
format	article
author	Saul Kivimäe Lino Saez Michael W Young
author_facet	Saul Kivimäe Lino Saez Michael W Young
author_sort	Saul Kivimäe
title	Activating PER repressor through a DBT-directed phosphorylation switch.
title_short	Activating PER repressor through a DBT-directed phosphorylation switch.
title_full	Activating PER repressor through a DBT-directed phosphorylation switch.
title_fullStr	Activating PER repressor through a DBT-directed phosphorylation switch.
title_full_unstemmed	Activating PER repressor through a DBT-directed phosphorylation switch.
title_sort	activating per repressor through a dbt-directed phosphorylation switch.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/26dd9adf4af44767ba443cacc77cf066
work_keys_str_mv	AT saulkivimae activatingperrepressorthroughadbtdirectedphosphorylationswitch AT linosaez activatingperrepressorthroughadbtdirectedphosphorylationswitch AT michaelwyoung activatingperrepressorthroughadbtdirectedphosphorylationswitch
_version_	1718414625911865344

Activating PER repressor through a DBT-directed phosphorylation switch.

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