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セミナーのご案内 David C. Klein Ph.D(National Institute of Child Health and Human Development NIH USA)

日時: 2月24日(木)午後3時から4時半まで
場所: 独立行政法人 産業技術総合研究所
つくば中央6−13 第6会議室
http://www.aist.go.jp/index_ja.html
発表者:David C. Klein Ph.D
Section on Neuroendocrinology
National Institute of Child Health and Human         Development NIH USA

演題:The Melatonin Rhythm Enzyme: Regulatory Role of Dual Site Binding to 14-3-3

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 K(m) for arylalkylamine substrate to approximately 30 muM. In contrast single-site pS205 binding increases the K(m) to approximately 1200 muM. Accordingly the switch from dual to single pS205 binding of AANAT to 14-3-3 changes the K(m) for substrates by approximately 40-fold. pS205 seems to be part of a previously unrecognized 14-3-3-binding motif-pS/pT (X(1-2))-COOH referred to here as mode III. (Proc Natl Acad Sci U S A. 2005 Jan 25;102(4):1222-7)