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- 1. コレラ菌感染の病因 pathogenesis of vibrio cholerae infection
- 2. 運動以外の好中球機能 neutrophil functions other than movement
English Journal
- Structural insights into the small G-protein Arl13B and implications for Joubert syndrome.
- Miertzschke M1, Koerner C1, Spoerner M2, Wittinghofer A1.Author information 1*Emeritus group A. Wittinghofer, Max-Planck-Institute for Molecular Physiology, BMZ, Otto-Hahn-Straße 15, 44227 Dortmund, Germany.2†Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.AbstractCiliopathies are human diseases arising from defects in primary or motile cilia. The small G-protein Arl13B (ADP-ribosylation factor-like 13B) localizes to microtubule doublets of the ciliary axoneme and is mutated in Joubert syndrome. Its GDP/GTP mechanistic cycle and the effect of its mutations in patients with Joubert syndrome remain elusive. In the present study we applied high resolution structural and biochemical approaches to study Arl13B. The crystal structure of Chlamydomonas rheinhardtii Arl13B, comprising the G-domain and part of its unique C-terminus, revealed an incomplete active site, and together with biochemical data the present study accounts for the absence of intrinsic GTP hydrolysis by this protein. The structure shows that the residues representing patient mutations R79Q and R200C are involved in stabilizing important intramolecular interactions. Our studies suggest that Arg79 is crucial for the GDP/GTP conformational change by stabilizing the large two-residue register shift typical for Arf (ADP-ribosylation factor) and Arl subfamily proteins. A corresponding mutation in Arl3 induces considerable defects in effector and GAP (GTPase-activating protein) binding, suggesting a loss of Arl13B function in patients with Joubert syndrome.
- The Biochemical journal.Biochem J.2014 Jan 15;457(2):301-11. doi: 10.1042/BJ20131097.
- Ciliopathies are human diseases arising from defects in primary or motile cilia. The small G-protein Arl13B (ADP-ribosylation factor-like 13B) localizes to microtubule doublets of the ciliary axoneme and is mutated in Joubert syndrome. Its GDP/GTP mechanistic cycle and the effect of its mutations in
- PMID 24168557
- Geometrical constraints limiting the poly(ADP-ribose) conformation investigated by molecular dynamics simulation.
- D'Annessa I, Coletta A, Desideri A.Author information Department of Biology and Centro di Bioinformatica e Biostatistica, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome, 00133, Italy.AbstractPoly(ADP-ribosylation) is a post-transductional modification that regulates protein's function. Most of the proteins subjected to this control mechanism belong to machineries involved in DNA damage repair, or DNA interacting proteins. Poly(ADP-ribose) polymers are long chains of even 100 monomer length that can be branched at several positions but, not withstanding its importance, nothing is known concerning its structure. To understand, which are the geometrical parameters that confer to the polymer the structural constraints that determine its interaction with the target proteins, we have performed molecular dynamics of three chains of different length, made by 5, 25, and 30 units, the last one being branched. Analysis of the simulations allowed us to identify the main intra- and inter-monomer dihedral angles that govern the structure of the polymer that however, does not reach a unique definite conformation. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 78-86, 2014.
- Biopolymers.Biopolymers.2014 Jan;101(1):78-86. doi: 10.1002/bip.22280.
- Poly(ADP-ribosylation) is a post-transductional modification that regulates protein's function. Most of the proteins subjected to this control mechanism belong to machineries involved in DNA damage repair, or DNA interacting proteins. Poly(ADP-ribose) polymers are long chains of even 100 monomer len
- PMID 23666795
- RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK.
- Dwane S, Durack E, O'Connor R, Kiely PA.Author information Department of Life Sciences and Materials and Surface Science Institute, University of Limerick, Limerick, Ireland.AbstractRACK1 binds proteins in a constitutive or transient manner and supports signal transmission by engaging in diverse and distinct signalling pathways. The emerging theme is that RACK1 functions as a signalling switch, recruiting proteins to form distinct molecular complexes. In focal adhesions, RACK1 is required for the regulation of FAK activity and for integrating a wide array of cellular signalling events including the integration of growth factor and adhesion signalling pathways. FAK is required for cell adhesion and migration and has a well-established role in neurite outgrowth and in the developing nervous system. However, the mechanism by which FAK activity is regulated in neurons remains unknown. Using neuronal cell lines, we determined that differentiation of these cells promotes an interaction between the scaffolding protein RACK1 and FAK. Disruption of the RACK1/FAK interaction leads to decreased neurite outgrowth suggesting a role for the interaction in neurite extension. We hypothesised that RACK1 recruits proteins to FAK, to regulate FAK activity in neuronal cells. To address this, we immunoprecipitated RACK1 from rat hippocampus and searched for interacting proteins by mass spectrometry. We identified AGAP2 as a novel RACK1-interacting protein. Having confirmed the RACK1-AGAP2 interaction biochemically, we show RACK1-AGAP2 to localise together in the growth cone of differentiated cells, and confirm that these proteins are in complex with FAK. This complex is disrupted when RACK1 expression is suppressed using siRNA or when mutants of RACK1 that do not interact with FAK are expressed in cells. Similarly, suppression of AGAP2 using siRNA leads to increased phosphorylation of FAK and increased cell adhesion resulting in decreased neurite outgrowth. Our results suggest that RACK1 scaffolds AGAP2 to FAK to regulate FAK activity and cell adhesion during the differentiation process.
- Cellular signalling.Cell Signal.2014 Jan;26(1):9-18. doi: 10.1016/j.cellsig.2013.08.036. Epub 2013 Sep 19.
- RACK1 binds proteins in a constitutive or transient manner and supports signal transmission by engaging in diverse and distinct signalling pathways. The emerging theme is that RACK1 functions as a signalling switch, recruiting proteins to form distinct molecular complexes. In focal adhesions, RACK1
- PMID 24056044
Japanese Journal
- アプリシア神経細胞における単量体G蛋白ADP-ribosylation factor (Arf) によるD_2型ドーパミン受容体刺激で発生するK^+電流応答の調整作用
- 渡辺 修二,原田 美里,川崎 敏 [他],藤田 玲子,木村 眞吾,渡辺 則之,佐々木 和彦
- 岩手医学雑誌 64(1), 35-49, 2012-04-01
- NAID 110009422778
- JB Reflections and Perspectives : The pioneering spirit of Takashi Sugimura : his studies of the biochemistry of poly(ADP-ribosylation) and of cancer
- Masutani Mitsuko
- Journal of Biochemistry 151(3), 221-228, 2012-03-00
- NAID 40019185902
- The Inhibitory G Protein Gi Identified as Pertussis Toxin-Catalyzed ADP-Ribosylation
- Katada Toshiaki
- Biological and Pharmaceutical Bulletin 35(12), 2103-2111, 2012
- … The action of PTX on isolated membranes required a cytosolic factor, nicotinamide adenine dinucleotide (NAD), and the uncoupling induced by PTX was shown to be due to the toxin-catalyzed ADP-ribosylation of a 41-kDa protein with NAD as another substrate. …
- NAID 130002480519
Related Links
- TNKS2 Histone Ribosylation Assay Kit (Biotin-labeled NAD+) (384reactions) 1kit \244,000 無 (未発注) 追加 BPS BPS バイオサイエンス BPS Bioscience Inc. 80573 Tankyrase-1, Histone Ribosylation Assay Kit, Biotin-Labeled 1kit ...
- ri·bo·syl·a·tion (rī'bō-sil-ā'shŭn), The covalent attachment of one or more ribosyl groups to a molecule (usually a macromolecule).
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★リンクテーブル★
| リンク元 | 「ribosylate」「リボシル化」「リボース化」 |
| 拡張検索 | 「ADP-ribosylation factor 1」「ADP-ribosylation factor」 |
「ribosylate」
- リボシル化する、リボース化する
「リボシル化」
「リボース化」
「ADP-ribosylation factor 1」
- 関
- ARF1
「ADP-ribosylation factor」
- 関
- ARF