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In Vivo phosphorylation site Mapping and Functional Characterization of Arabidopsis Phototropin 1

Molecular Plant 2008年第1期1卷 178-194页

作者： Stuart Sullivan Catriona E. Thomson Douglas J. Lamont Matthew A. Jones John M. Christie Plant Science Group Division of Biochemistry and Molecular Biology. Institute of Biomedical and Life Sciences University of Glasgow. University Avenue. Glasgow Scotland UK FingerPrints Proteomics Facility Post-Genomics and Molecular Interactions Centre. School of Life Sciences MSI/WTB/CIR Complex University of Dundee. Dundee Scotland UK

Phototropins （phot1 and phot2） are blue-light receptor kinases controlling a range of responses that optimize the photosynthetic efficiency of plants. Light sensing is mediated by two flavin-binding motifs, known as LOVl and LOV2, located within the N-terminal region of the protein. Photoexcitation via LOV2 leads to activation of the C-terminal kinase domain and consequently receptor autophosphorylation. However, knowledge of the in-vivo phosphorylation sites for Arabidopsis phototropins is lacking and has impeded progress in elucidating the functional significance of receptor phos- phorylation. We have purified photl from Arabidopsis and identified the in-vivo sites of receptor phosphorylation by liquid chromatography tandem mass spectrometry. Arabidopsis-derived photl binds flavin mononucleotide as chromophore and is phosphorylated at four major sites located upstream of LOV2 （Ser^58, Ser^85, Ser^350, and Ser^410）, three of which are induced by blue light. Nevertheless, structure-function analysis indicates that the biological activity of photl can be attributed to a modular unit comprising the LOV2-kinase region of the protein. Thus, peptide regions upstream of LOV2, including the sites of receptor phosphorylation identified here, do not appear to be important for receptor signaling. By contrast, these regions may be necessary for maximizing stomatal performance and possibly light-induced relocalization of photl.

关键词： MODULAR UNIT Phototropins chromophores phosphorylation site Function analysis Upstream photosynthetic efficiency Arabidopsis PHOSPHONATION Receptor Signaling Flavin Mononucleotide Receptor

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Proteomic analysis of mTOR inhibition- mediated phosphorylation changes in ribosomal proteins and eukaryotic translation initiation factors

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Protein & Cell 2016年第7期7卷 533-537页

作者： Xu Jiang Shan Feng Yuling Chen Yun Feng Haiteng Deng MOE Key Laboratory of Bioinformatics School of Life SciencesTsinghua University Beijing 100084 China

Dear Editor, The mammalian target of rapamycin （mTOR）, as a critical energy sensor and cell-growth regulator, controls protein synthesis, autophagy and many important cellular processes through forming functional distinct complexes, mTORC1 and mTORC2, mTORC1 that is sensitive to rapamycin, regulates cell growth and protein synthesis, while mTORC2 that is insensitive to rapamycin, regulates cellular metabolism and the cytoskeletal organization （Gingras et al., 2001; Hay and Sonenberg, 2004）. Translation initiation is the rate-limiting step in protein synthesis, which proceeds through a multi- step process that can be divided into three major steps. First, eukaryotic translation initiation factor 2 （elF2） binds with GTP and methionyl-tRNA to form the ternary complex, which further binds to 40S ribosomal subunit with the help of elF1, elF1A, elF3 and elF5 resulting the preinitiation complex （PIC）. Second, the PIC binds to mRNA which is unwinded by the elF4F complex （including elF4E, elF4G, elF4A, elF4B）.

关键词： phosphorylation site Rapamycin Treatment Eukaryotic Translation Initiation Factor Mediate phosphorylation phosphorylation Peptide

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Structural biology study of human TNF receptor associated factor 4 TRAF domain

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Protein & Cell 2013年第9期4卷 687-694页

作者： Fengfeng Niu Heng Ru Wei Ding Songying Ouyang Zhi-Jie Liu National Laboratory of Biomacromolecules Institute of BiophysicsChinese Academy of SciencesBeijing 100101China Institute of Molecular and Clinical Medicine Kunming Medical UniversityKunming 650500China University of Chinese Academy of Sciences Beijing 100049China

TRAF4 is a unique member of TRAF family,which is es-sential for innate immune response,nervous system and other *** addition to being an adaptor protein,TRAF4 was identifi ed as a regulator protein in recent *** have determined the crystal structure of TRAF domain of TRAF4(residues 292-466)at 2.60Åresolution by X-ray crystallography *** trimericly assembled TRAF4 resembles a mushroom shape,containing a super helical“stalk”which is made of three right-handed intertwinedαhelixes and a C-terminal“cap”,which is divided at resi-due L302 as a *** to other TRAFs,both intermolecular hydrophobic interaction in super helical“stalk”and hydrogen bonds in“cap”regions contribute directly to the formation of TRAF4 ***,differ-ing from other TRAFs,there is an additional fl exible loop(residues 421-426),which contains a previously identifi ed phosphorylated site S426 exposing on the *** S426 was reported to be phosphorylated by IKKαwhich is the pre-requisite for TRAF4-NOD2 complex formation and thus to inhibit NOD2-induced NF-κB ***,the crystal structure of TRAF4-TRAF is valuable for under-standing its molecular basis for its special function and provides structural information for further studies.

关键词： TRAF4 TRAF domain crystal structure ad-ditional loop phosphorylation site

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Molecular Basis and Regulation of Ammonium Transporter in Rice

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Rice science 2009年第4期16卷 314-322页

作者： LI Bao-zhen Mike MERRICK LI Su-mei LI Hong-ying ZHU Shu-wen SHI Wei-ming Su Yan-hua State Key Laboratory of Soil and Sustainable Agriculture Institute of Soil Science Chinese Academy of Sciences Nanjing 210008 China Department of Molecular Microbiology John Innes Centre Colney Lane Norwich NR4 7UH UK

Rice grows in flooded paddy fields and takes up ammonium as the preferred nitrogen （N） source. Ammonium uptake is facilitated by a family of integral membrane proteins known as ammonium transporters found in all domains of life. However, the molecular mechanism and functional characteristics of the ammonium transporters （AMT） in rice have not been determined in detail yet. In this review, we report a genome-wide search for AMT genes in rice, resulting in the increase of the number of potential AMT proteins to at least 12, including members of both the alpha and beta sub-groups. Analysis of the predicted protein sequences for the 12 OsAMT proteins identified many conserved phosphorylation sites in both the alpha and beta group members, which could potentially play a role in controlling the activity of the transporters. Present knowledge of the expression of rice AMT genes is also summarized in detail. Future studies should focus on the structural and functional characteristics of OsAMT proteins to provide insight into the mechanism of ammonium uptake and its regulation in rice. Such research could improve utilization and decrease wastage of N fertilizer in rice cultivation.

关键词： rice ammonium transporter expression regulation phosphorylation site

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