<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Schneider K</submitter><funding>Swiss National Science Foundation</funding><pagination>1138-44</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3512403</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(12)</volume><pubmed_abstract>In mammals, transcriptional autorepression by Period (PER) and Cryptochrome (CRY) protein complexes is essential for the generation of circadian rhythms. We have identified CAVIN-3 as a new, cytoplasmic PER2-interacting protein influencing circadian clock properties. Thus, CAVIN-3 loss- and gain-of-function shortened and lengthened, respectively, the circadian period in fibroblasts and affected PER:CRY protein abundance and interaction. While depletion of protein kinase Cδ (PKCδ), a known partner of CAVIN-3, had little effect on circadian gene expression, CAVIN-3 required the PKCδ-binding site to exert its effect on period length. This suggests the involvement of yet uncharacterized protein kinases. Finally, CAVIN-3 activity in circadian gene expression was independent of caveolae.</pubmed_abstract><journal>EMBO reports</journal><pubmed_title>CAVIN-3 regulates circadian period length and PER:CRY protein abundance and interactions.</pubmed_title><pmcid>PMC3512403</pmcid><funding_grant_id>128399</funding_grant_id><funding_grant_id>113565</funding_grant_id><funding_grant_id>128656</funding_grant_id><pubmed_authors>Kurzchalia T</pubmed_authors><pubmed_authors>Schibler U</pubmed_authors><pubmed_authors>Gatfield D</pubmed_authors><pubmed_authors>Schneider K</pubmed_authors><pubmed_authors>Kocher T</pubmed_authors><pubmed_authors>Andersin T</pubmed_authors></additional><is_claimable>false</is_claimable><name>CAVIN-3 regulates circadian period length and PER:CRY protein abundance and interactions.</name><description>In mammals, transcriptional autorepression by Period (PER) and Cryptochrome (CRY) protein complexes is essential for the generation of circadian rhythms. We have identified CAVIN-3 as a new, cytoplasmic PER2-interacting protein influencing circadian clock properties. Thus, CAVIN-3 loss- and gain-of-function shortened and lengthened, respectively, the circadian period in fibroblasts and affected PER:CRY protein abundance and interaction. While depletion of protein kinase Cδ (PKCδ), a known partner of CAVIN-3, had little effect on circadian gene expression, CAVIN-3 required the PKCδ-binding site to exert its effect on period length. This suggests the involvement of yet uncharacterized protein kinases. Finally, CAVIN-3 activity in circadian gene expression was independent of caveolae.</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Dec</publication><modification>2025-04-19T12:22:24.339Z</modification><creation>2019-03-27T01:01:20Z</creation></dates><accession>S-EPMC3512403</accession><cross_references><pubmed>23079727</pubmed><doi>10.1038/embor.2012.158</doi></cross_references></HashMap>