Linked Life Data

16319317

Source:http://linkedlifedata.com/resource/pubmed/id/16319317

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
48
pubmed:dateCreated
2005-12-1
pubmed:abstractText
Phosphorylation plays a key role in the precise timing of circadian clocks. Daily rhythms of phosphorylation of the Drosophila circadian clock component PERIOD (PER) were first described more than a decade ago, yet little is known about their phosphorylation sites and their function in circadian behavior. Here we show that serines 151 and 153 in PER are required for robust in vitro phosphorylation by the casein kinase 2 (CK2) holoenzyme, a cytoplasmic kinase shown to be involved in circadian rhythms. Mutation of these sites in transgenic flies results in significant period lengthening of behavioral rhythms, altered PER rhythms, and delayed PER nuclear localization in circadian pacemaker neurons. In many respects, mutation of these phosphorylation sites phenocopies mutation of the catalytic subunit of CK2. We propose that CK2 phosphorylation at these sites triggers PER nuclear localization.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
30
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11175-83
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
In vivo circadian function of casein kinase 2 phosphorylation sites in Drosophila PERIOD.
pubmed:affiliation
Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural