An Intramolecular Disulfide Bridge as a Catalytic Switch for Serotonin N-Acetyltransferase

Tsuboi, Seiji; Kotani, Yasunori; Ogawa, Kenichi; Hatanaka, Tadashi; Yatsushiro, Shouki; Otsuka, Masato; Moriyama, Yoshinori

doi:10.1074/jbc.m203305200

Cited by 13 publications

(4 citation statements)

References 32 publications

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“…AA-NAT phosphorylation is a crucial step not only because it allows binding to the 14-3-3 protein and activation, but also because it shields AA-NAT from destruction by cytosolic proteasomes Ganguly et al, 2002). Additionally, an intramolecular disulfide bond between the Cys -61 and Cys 177 , formed upon oxidation and cleaved upon reduction, is proposed 342 SIMONNEAUX AND RIBELAYGA to act as a catalytic switch for AA-NAT activation (Tsuboi et al, 2002).…”

Section: F Arylalkylamine-n-acetyltransferasementioning

confidence: 99%

Generation of the Melatonin Endocrine Message in Mammals: A Review of the Complex Regulation of Melatonin Synthesis by Norepinephrine, Peptides, and Other Pineal Transmitters

2003

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Section: F Arylalkylamine-n-acetyltransferasementioning

confidence: 99%

Generation of the Melatonin Endocrine Message in Mammals: A Review of the Complex Regulation of Melatonin Synthesis by Norepinephrine, Peptides, and Other Pineal Transmitters

2003

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“…It also shields AANAT from proteins involved in dephosphorylation and degradation and may also prevent thiol-dependent inactivation (24,25,27,30,(47)(48)(49).…”

Section: Structure and Functionmentioning

confidence: 99%

Arylalkylamine N-Acetyltransferase: “the Timezyme”

Klein

2007

Journal of Biological Chemistry

374

347

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Arylalkylamine N-acetyltransferase controls daily changes in melatonin production by the pineal gland and thereby plays a unique role in biological timing in vertebrates. Arylalkylamine N-acetyltransferase is also expressed in the retina, where it may play other roles in addition to signaling, including neurotransmission and detoxification. Large changes in activity reflect cyclic 3,5-adenosine monophosphate-dependent phosphorylation of arylalkylamine N-acetyltransferase, leading to formation of a regulatory complex with 14-3-3 proteins. This activates the enzyme and prevents proteosomal proteolysis. The conserved features of regulatory systems that control arylalkylamine N-acetyltransferase are a circadian clock and environmental lighting.Arylalkylamine N-acetyltransferase (AANAT; EC 2.1.3.87) 2 plays a unique role in vertebrate biology by controlling the rhythmic production of melatonin in the pineal gland ( Fig. 1) (1). Activity increases 10-to 100-fold at night, causing an increase in the production and release of melatonin. The dynamics of AANAT activity are remarkable: the doubling time is ϳ15 min at night, and the halving time of the decrease that follows a night 3 light transition is ϳ3.5 min (2, 3). Circulating melatonin levels parallel changes in synthesis and release, due to rapid clearance by the liver (1).The rhythmic pattern of activity in the melatonin pathway is a conserved feature of vertebrate biology, consistent with the role of melatonin as the vertebrate hormone of time, i.e. high levels signal night and low levels signal day. Although this signaling pattern is conserved, it is used in a variety of species-dependent ways to optimally control seasonal and daily changes in physiology (1). The unique role that AANAT plays in vertebrate time keeping justifies the title of "the Timezyme." Our knowledge of the biological chemistry of AANAT is summarized in this overarching review. Aanat Genes and EvolutionThe AANAT Family-Aanat and Aanat homologs form the AANAT family, which is part of the large Gcn5-related acetyltransferase (GNAT) superfamily (4, 5). All GNAT family members share common structural features associated with acetyl coenzyme A (AcCoA) binding; in addition, each member family has unique features reflecting substrate specificity for each of a wide range of substrates (e.g. aminoglycosides, diamines, puromycin, histones, and arylalkylamines). The GNAT superfamily also includes another arylalkylamine N-acetyltransferase family, represented by dopamine N-aceyltransferase (Dat), which is expressed in Drosophila melanogaster (6). Dat is not involved time keeping; rather, it functions in cuticle sclerotization and neurotransmission (6). DAT and AANAT family members have not been found in the same genome.AANAT family members have only been found in Grampositive bacteria, fungi, algae, cephalochordates, and vertebrates; family members are not found in higher plants, insects, nematodes, or urochordates (7). This distribution may be explained by the initial appearance of the ancestral Aanat in ...

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“…By generating glutathione (GSH), these glutathione peroxidases can act as scavengers of reactive oxygen species and regulate the oxidative state of proteins together with a transmembrane thioredoxin (Tmx2b) (Yoshihara, et al 2010 ). For the NAT8 and rbp4a, these two proteins are primarily indirectly involved in the process of redox state change (Hammerling 2016 ; Tsuboi et al 2002 ; Zanotto-Filho et al 2008 ).…”

Section: Discussionmentioning

confidence: 99%

Transcriptomic and proteomic analyses provide insights into the adaptive responses to the combined impact of salinity and alkalinity in Gymnocypris przewalskii

Wei

Liang

Tian³

et al. 2022

Bioresour. Bioprocess.

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Gymnocypris przewalskii is the only high-land endemic teleost living in Qinghai Lake, the largest saline–alkaline lake in China. Its osmoregulatory physiology remains elusive due to a lack of precise identification of the response proteins. In the present study, DIA/SWATH was used to identify differentially expressed proteins (DEPs) under alkaline (pH = 10.1, carbonate buffer), saline (12‰, sodium chloride), and saline–alkaline [carbonate buffer (pH = 10.1) plus 11‰ sodium chloride] stresses. A total of 66,056 unique peptides representing 7,150 proteins and 230 DEPs [the false discovery rate (FDR) ≤ 0.05, fold change (FC) ≥ 1.5] were identified under different stresses. Comparative analyses of the proteome and transcriptome indicated that over 86% of DEPs did not show consistent trends with mRNA. In addition to consistent enrichment results under different stresses, the specific DEPs involved in saline–alkaline adaptation were primarily enriched in functions of homeostasis, hormone synthesis and reactions of defense response, complement activation and reproductive development. Meanwhile, a protein–protein interaction (PPI) network analysis of these specific DEPs indicated that the hub genes were ITGAX, MMP9, C3, F2, CD74, BTK, ANXA1, NCKAP1L, and CASP8. This study accurately isolated the genes that respond to stress, and the results could be helpful for understanding the physiological regulation mechanisms regarding salinity, alkalinity, and salinity–alkalinity interactions. Graphical Abstract

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An Intramolecular Disulfide Bridge as a Catalytic Switch for Serotonin N-Acetyltransferase

Cited by 13 publications

References 32 publications

Generation of the Melatonin Endocrine Message in Mammals: A Review of the Complex Regulation of Melatonin Synthesis by Norepinephrine, Peptides, and Other Pineal Transmitters

Generation of the Melatonin Endocrine Message in Mammals: A Review of the Complex Regulation of Melatonin Synthesis by Norepinephrine, Peptides, and Other Pineal Transmitters

Arylalkylamine N-Acetyltransferase: “the Timezyme”

Transcriptomic and proteomic analyses provide insights into the adaptive responses to the combined impact of salinity and alkalinity in Gymnocypris przewalskii

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