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http://purl.uniprot.org/citations/15644438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15644438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15644438http://www.w3.org/2000/01/rdf-schema#comment"The nocturnal increase in circulating melatonin in vertebrates is regulated by the activity of arylalkylamine N-acetyltransferase (AANAT), the penultimate enzyme in the melatonin pathway (serotonin --> N-acetylserotonin --> melatonin). Large changes in activity are linked to cyclic AMP-dependent protein kinase-mediated phosphorylation of AANAT T31. Phosphorylation of T31 promotes binding of AANAT to the dimeric 14-3-3 protein, which activates AANAT by increasing arylalkylamine affinity. In the current study, a putative second AANAT cyclic AMP-dependent protein kinase phosphorylation site, S205, was found to be approximately 55% phosphorylated at night, when T31 is approximately 40% phosphorylated. These findings indicate that ovine AANAT is dual-phosphorylated. Moreover, light exposure at night decreases T31 and S205 phosphorylation, consistent with a regulatory role of both sites. AANAT peptides containing either T31 or S205 associate with 14-3-3zeta in a phosphorylation-dependent manner; binding through phosphorylated (p)T31 is stronger than that through pS205, consistent with the location of only pT31 in a mode I binding motif, one of two recognized high-affinity 14-3-3-binding motifs AANAT protein binds to 14-3-3zeta through pT31 or pS205. Two-site binding lowers the Km for arylalkylamine substrate to approximately 30 microM. In contrast, single-site pS205 binding increases the Km to approximately 1,200 microM. Accordingly, the switch from dual to single pS205 binding of AANAT to 14-3-3 changes the Km for substrates by approximately 40-fold. pS205 seems to be part of a previously unrecognized 14-3-3-binding motif-pS/pT (X1-2)-COOH, referred to here as mode III."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0406871102"xsd:string
http://purl.uniprot.org/citations/15644438http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0406871102"xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Chemineau P."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Chemineau P."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Ganguly S."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Ganguly S."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Ho A."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Ho A."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Klein D.C."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Klein D.C."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Malpaux B."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Malpaux B."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Weller J.L."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/author"Weller J.L."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/pages"1222-1227"xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/pages"1222-1227"xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/title"Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205."xsd:string
http://purl.uniprot.org/citations/15644438http://purl.uniprot.org/core/title"Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205."xsd:string
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