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Article: Casein kinase 1delta functions at the centrosome and Golgi to promote ciliogenesis

TitleCasein kinase 1delta functions at the centrosome and Golgi to promote ciliogenesis
Authors
KeywordsA Kinase Anchor Proteins/biosynthesis/*metabolism
Animals
Binding Sites
Carrier Proteins
Casein Kinase Idelta/*antagonists & inhibitors/genetics
Cell Cycle Proteins/metabolism
Cell Line
Centrosome/*metabolism
Cilia/*metabolism
Golgi Apparatus/*metabolism
Humans
Mice
Mice, Knockout
Microtubule-Associated Proteins/biosynthesis/*metabolism
Microtubules/metabolism
Nuclear Proteins/metabolism
Protein Transport
RNA Interference
RNA, Small Interfering
Retina/cytology
Signal Transduction/genetics
TRPP Cation Channels/metabolism
Telomerase/genetics
rab GTP-Binding Proteins/metabolism
Issue Date2014
Citation
Molecular Biology of the Cell, 2014, v. 25 n. 10, p. 1629-1640 How to Cite?
AbstractInhibition of casein kinase 1 delta (CK1delta) blocks primary ciliogenesis in human telomerase reverse transcriptase immortalized retinal pigmented epithelial and mouse inner medullary collecting duct cells-3. Mouse embryonic fibroblasts (MEFs) and retinal cells from Csnk1d (CK1delta)-null mice also exhibit ciliogenesis defects. CK1delta catalytic activity and centrosomal localization signal (CLS) are required to rescue cilia formation in MEFs(Csnk1d null). Furthermore, expression of a truncated derivative containing the CLS displaces full-length CK1delta from the centrosome and decreases ciliary length in control MEFs, suggesting that centrosomal CK1delta has a role in ciliogenesis. CK1delta inhibition also alters pericentrosomal or ciliary distribution of several proteins involved in ciliary transport, including Ras-like in rat brain-11A, Ras-like in rat brain-8A, centrosomal protein of 290 kDa, pericentriolar material protein 1, and polycystin-2, as well as the Golgi distribution of its binding partner, A-kinase anchor protein 450 (AKAP450). As reported for AKAP450, CK1delta was required for microtubule nucleation at the Golgi and maintenance of Golgi integrity. Overexpression of an AKAP450 fragment containing the CK1delta-binding site inhibits Golgi-derived microtubule nucleation, Golgi distribution of intraflagellar transport protein 20 homologue, and ciliogenesis. Our results suggest that CK1delta mediates primary ciliogenesis by multiple mechanisms, one involving its centrosomal function and another dependent on its interaction with AKAP450 at the Golgi, where it is important for maintaining Golgi organization and polarized trafficking of multiple factors that mediate ciliary transport.
Persistent Identifierhttp://hdl.handle.net/10722/208433
ISSN

 

DC FieldValueLanguage
dc.contributor.authorGreer, YEen_US
dc.contributor.authorWestlake, CJen_US
dc.contributor.authorGao, Ben_US
dc.contributor.authorBharti, Ken_US
dc.contributor.authorShiba, Yen_US
dc.contributor.authorXavier, CPen_US
dc.contributor.authorPazour, GJen_US
dc.contributor.authorYang, Yen_US
dc.contributor.authorRubin, JSen_US
dc.date.accessioned2015-03-11T03:00:51Z-
dc.date.available2015-03-11T03:00:51Z-
dc.date.issued2014en_US
dc.identifier.citationMolecular Biology of the Cell, 2014, v. 25 n. 10, p. 1629-1640en_US
dc.identifier.issn1939-4586en_US
dc.identifier.urihttp://hdl.handle.net/10722/208433-
dc.description.abstractInhibition of casein kinase 1 delta (CK1delta) blocks primary ciliogenesis in human telomerase reverse transcriptase immortalized retinal pigmented epithelial and mouse inner medullary collecting duct cells-3. Mouse embryonic fibroblasts (MEFs) and retinal cells from Csnk1d (CK1delta)-null mice also exhibit ciliogenesis defects. CK1delta catalytic activity and centrosomal localization signal (CLS) are required to rescue cilia formation in MEFs(Csnk1d null). Furthermore, expression of a truncated derivative containing the CLS displaces full-length CK1delta from the centrosome and decreases ciliary length in control MEFs, suggesting that centrosomal CK1delta has a role in ciliogenesis. CK1delta inhibition also alters pericentrosomal or ciliary distribution of several proteins involved in ciliary transport, including Ras-like in rat brain-11A, Ras-like in rat brain-8A, centrosomal protein of 290 kDa, pericentriolar material protein 1, and polycystin-2, as well as the Golgi distribution of its binding partner, A-kinase anchor protein 450 (AKAP450). As reported for AKAP450, CK1delta was required for microtubule nucleation at the Golgi and maintenance of Golgi integrity. Overexpression of an AKAP450 fragment containing the CK1delta-binding site inhibits Golgi-derived microtubule nucleation, Golgi distribution of intraflagellar transport protein 20 homologue, and ciliogenesis. Our results suggest that CK1delta mediates primary ciliogenesis by multiple mechanisms, one involving its centrosomal function and another dependent on its interaction with AKAP450 at the Golgi, where it is important for maintaining Golgi organization and polarized trafficking of multiple factors that mediate ciliary transport.en_US
dc.languageengen_US
dc.relation.ispartofMolecular Biology of the Cellen_US
dc.subjectA Kinase Anchor Proteins/biosynthesis/*metabolismen_US
dc.subjectAnimalsen_US
dc.subjectBinding Sitesen_US
dc.subjectCarrier Proteinsen_US
dc.subjectCasein Kinase Idelta/*antagonists & inhibitors/geneticsen_US
dc.subjectCell Cycle Proteins/metabolismen_US
dc.subjectCell Lineen_US
dc.subjectCentrosome/*metabolismen_US
dc.subjectCilia/*metabolismen_US
dc.subjectGolgi Apparatus/*metabolismen_US
dc.subjectHumansen_US
dc.subjectMiceen_US
dc.subjectMice, Knockouten_US
dc.subjectMicrotubule-Associated Proteins/biosynthesis/*metabolismen_US
dc.subjectMicrotubules/metabolismen_US
dc.subjectNuclear Proteins/metabolismen_US
dc.subjectProtein Transporten_US
dc.subjectRNA Interferenceen_US
dc.subjectRNA, Small Interferingen_US
dc.subjectRetina/cytologyen_US
dc.subjectSignal Transduction/geneticsen_US
dc.subjectTRPP Cation Channels/metabolismen_US
dc.subjectTelomerase/geneticsen_US
dc.subjectrab GTP-Binding Proteins/metabolismen_US
dc.titleCasein kinase 1delta functions at the centrosome and Golgi to promote ciliogenesisen_US
dc.typeArticleen_US
dc.identifier.emailGao, B: gaobo@hku.hken_US
dc.identifier.authorityGao, B=rp02012en_US
dc.identifier.doi10.1091/mbc.E13-10-0598en_US
dc.identifier.pmid24648492-
dc.identifier.scopuseid_2-s2.0-84901207762-
dc.identifier.volume25en_US
dc.identifier.issue10en_US
dc.identifier.spage1629en_US
dc.identifier.epage1640en_US

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