関: syntaxin

WordNet

a trap for birds or small mammals; often has a slip noose (同)gin, noose
a surgical instrument consisting of wire hoop that can be drawn tight around the base of polyps or small tumors to sever them; used especially in body cavities
strings stretched across the lower head of a snare drum; they make a rattling sound when the drum is hit
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
the 17th letter of the Roman alphabet (同)q
the last imperial dynasty of China (from 1644 to 1912) which was overthrown by revolutionaries; during the Qing dynasty China was ruled by the Manchu (同)Qing dynasty, Ch''ing, Ch''ing dynasty, Manchu, Manchu dynasty

PrepTutorEJDIC

(小動物を捕らえる)『わな』《+『for』+『名』》 / (人を陥れる)『わな』,落とし穴《+『for』+『名』》 / 〈小動物〉‘を'わなにかける〈人〉‘を'わなにかける,陥れる
(小太鼓の)さわり弦,響線
蛋白(たんばく)質
(チェスの)queen

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1. 適応細胞性免疫応答 the adaptive cellular immune response
2. 成人における肺炎球菌ワクチン pneumococcal vaccination in adults
3. 炎症性腸疾患における大腸癌のサーべイランス colorectal cancer surveillance in inflammatory bowel disease
4. 腹部大動脈瘤の血管内修復 endovascular repair of abdominal aortic aneurysm
5. 薬理ゲノム学の概要 overview of pharmacogenomics

English Journal

Interactomics of Qa-SNARE in Arabidopsis thaliana.

Fujiwara M1, Uemura T, Ebine K, Nishimori Y, Ueda T, Nakano A, Sato MH, Fukao Y.Author information 1Plant Global Educational Project, Nara Institute of Science and Technology, Ikoma, 630-0192 Japan.AbstractMembrane trafficking in plants is involved in cellular development and the adaptation to various environmental changes. SNARE proteins mediate the fusion between vesicles and organelles to facilitate transport cargo proteins in cells. To further characterize SNARE protein networks in cells, we carried out interactome analysis of SNARE proteins using 12 transgenic Arabidopsis thaliana plants expressing GFP-tagged Qa-SNAREs (SYP111, SYP121, SYP122, SYP123, SYP132, SYP21, SYP22, SYP31, SYP32, SYP41, SYP42 and SYP43). Microsomal fractions were prepared from each transgenic root, and subjected to immunoprecipitation (IP) using micro-magnetic beads coupled to anti-GFP antibodies. To identify Qa-SNARE-interacting proteins, all IP products were then subjected to mass spectrometric (IP-MS) analysis. The IP-MS data revealed not only known interactions of SNARE proteins, but also unknown interactions. The IP-MS results were next categorized by gene ontology analysis. Data revealed that categories of cellular component organization, cytoskeleton and endosome were enriched in the SYP2, SYP3 and SYP4 groups. In contrast, transporter activity was classified specifically in the SYP132 group. We also identified a novel interaction between SYP22 and VAMP711, which was validated using co-localization analysis with confocal microscopy and immunoprecipitation. Additional novel SNARE-interacting proteins play roles in vesicle transport and lignin biosynthesis, and were identified as membrane microdomain-related proteins. We propose that Qa-SNARE interactomics is useful for understanding SNARE interactions across the whole cell.
Plant & cell physiology.Plant Cell Physiol.2014 Feb 19. [Epub ahead of print]
Membrane trafficking in plants is involved in cellular development and the adaptation to various environmental changes. SNARE proteins mediate the fusion between vesicles and organelles to facilitate transport cargo proteins in cells. To further characterize SNARE protein networks in cells, we carri
PMID 24556609

Syntaxin11 serves as a t-SNARE for the fusion of lytic granules in human cytotoxic T lymphocytes.

Halimani M1, Pattu V, Marshall MR, Chang HF, Matti U, Jung M, Becherer U, Krause E, Hoth M, Schwarz EC, Rettig J.Author information 1Institut für Physiologie, Universität des Saarlandes, Homburg/Saar, Germany.AbstractCTLs kill target cells via fusion of lytic granules (LGs) at the immunological synapse (IS). Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) function as executors of exocytosis. The importance of SNAREs in CTL function is evident in the form of familial hemophagocytic lymphohistiocytosis type 4 that is caused by mutations in Syntaxin11 (Stx11), a Qa-SNARE protein. Here, we investigate the molecular mechanism of Stx11 function in primary human effector CTLs with high temporal and spatial resolution. Downregulation of endogenous Stx11 resulted in a complete inhibition of LG fusion that was paralleled by a reduction in LG dwell time at the IS. Dual color evanescent wave imaging suggested a sequential process, in which first Stx11 is transported to the IS through a subpopulation of recycling endosomes. The resulting Stx11 clusters at the IS then serve as a platform to mediate fusion of arriving LGs. We conclude that Stx11 functions as a t-SNARE for the final fusion of LG at the IS, explaining the severe phenotype of familial hemophagocytic lymphohistiocytosis type 4 on a molecular level.
European journal of immunology.Eur J Immunol.2014 Feb;44(2):573-84. doi: 10.1002/eji.201344011. Epub 2013 Dec 16.
CTLs kill target cells via fusion of lytic granules (LGs) at the immunological synapse (IS). Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) function as executors of exocytosis. The importance of SNAREs in CTL function is evident in the form of familial hemophagocytic
PMID 24227526

Munc18-2 and syntaxin 3 control distinct essential steps in mast cell degranulation.

Brochetta C1, Suzuki R, Vita F, Soranzo MR, Claver J, Madjene LC, Attout T, Vitte J, Varin-Blank N, Zabucchi G, Rivera J, Blank U.Author information 1INSERM Unité Mixte de Recherche-699, 75018 Paris, France;AbstractMast cell degranulation requires N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) and mammalian uncoordinated18 (Munc18) fusion accessory proteins for membrane fusion. However, it is still unknown how their interaction supports fusion. In this study, we found that small interfering RNA-mediated silencing of the isoform Munc18-2 in mast cells inhibits cytoplasmic secretory granule (SG) release but not CCL2 chemokine secretion. Silencing of its SNARE-binding partner syntaxin 3 (STX3) also markedly inhibited degranulation, whereas combined knockdown produced an additive inhibitory effect. Strikingly, while Munc18-2 silencing impaired SG translocation, silencing of STX3 inhibited fusion, demonstrating unique roles of each protein. Immunogold studies showed that both Munc18-2 and STX3 are located on the granule surface, but also within the granule matrix and in small nocodazole-sensitive clusters of the cytoskeletal meshwork surrounding SG. After stimulation, clusters containing both effectors were detected at fusion sites. In resting cells, Munc18-2, but not STX3, interacted with tubulin. This interaction was sensitive to nocodazole treatment and decreased after stimulation. Our results indicate that Munc18-2 dynamically couples the membrane fusion machinery to the microtubule cytoskeleton and demonstrate that Munc18-2 and STX3 perform distinct, but complementary, functions to support, respectively, SG translocation and membrane fusion in mast cells.
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2014 Jan 1;192(1):41-51. doi: 10.4049/jimmunol.1301277. Epub 2013 Dec 9.
Mast cell degranulation requires N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) and mammalian uncoordinated18 (Munc18) fusion accessory proteins for membrane fusion. However, it is still unknown how their interaction supports fusion. In this study, we found that small interfe
PMID 24323579