Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김희선 | * |
dc.contributor.author | 안정혁 | * |
dc.date.accessioned | 2016-08-28T12:08:25Z | - |
dc.date.available | 2016-08-28T12:08:25Z | - |
dc.date.issued | 2011 | * |
dc.identifier.issn | 1932-6203 | * |
dc.identifier.other | OAK-8098 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/222055 | - |
dc.description.abstract | Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that dephosphorylates Ser40 is protein phosphatase-2A (PP2A). A recent study has also linked protein kinase C to the dephosphorylation of Ser40 [1] but the mechanism is unclear. PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellular localization and substrate selection. In the current study, we find that protein kinase C is able to phosphorylate a key regulatory site in the B56δ subunit leading to activation of PP2A. In turn, activation of the B56δ-containing heterotrimeric form of PP2A is responsible for enhanced dephosphorylation of Ser40 of tyrosine hydroylase in response to stimulation of PKC. In support of this mechanism, down-regulation of B56δ expression in N27 cells using RNAi was found to increase dopamine synthesis. Together these studies reveal molecular details of how protein kinase C is linked to reduced tyrosine hydroxylase activity via control of PP2A, and also add to the complexity of protein kinase/protein phosphatase interactions. © 2011 Ahn et al. | * |
dc.language | English | * |
dc.title | Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A | * |
dc.type | Article | * |
dc.relation.issue | 10 | * |
dc.relation.volume | 6 | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.journaltitle | PLoS ONE | * |
dc.identifier.doi | 10.1371/journal.pone.0026292 | * |
dc.identifier.wosid | WOS:000296513200015 | * |
dc.identifier.scopusid | 2-s2.0-80054834577 | * |
dc.author.google | Ahn J.-H. | * |
dc.author.google | Kim Y. | * |
dc.author.google | Kim H.-S. | * |
dc.author.google | Greengard P. | * |
dc.author.google | Nairn A.C. | * |
dc.contributor.scopusid | 김희선(57191372551) | * |
dc.contributor.scopusid | 안정혁(35081632000) | * |
dc.date.modifydate | 20240123125644 | * |