アダプタータンパク質複合体
WordNet
- complicated in structure; consisting of interconnected parts; "a complex set of variations based on a simple folk melody"; "a complex mass of diverse laws and customs"
- a compound described in terms of the central atom to which other atoms are bound or coordinated (同)coordination_compound
- a conceptual whole made up of complicated and related parts; "the complex of shopping malls, houses, and roads created a new town" (同)composite
- (psychoanalysis) a combination of emotions and impulses that have been rejected from awareness but still influence a persons behavior
- make fit for, or change to suit a new purpose; "Adapt our native cuisine to the available food resources of the new country" (同)accommodate
- 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"
PrepTutorEJDIC
- 『いくつかの部分から成る』,複合の,合成の / 『複雑な』,入りくんだ,こみいった(complicated) / 複合体,合成物 / コンプレックス,複合(抑圧されて心に残った複雑なしこり)
- (…に)…'を'『適応させる』,適合させる《+『名』+『to』+『名』(do『ing』)》 / (…向きに)〈小説・戯曲など〉'を'『脚色する』,翻案する,書きかえる《+『名』+『for』+『名』》 / (環境などに)適応する,順応する《+『to』+『名』》
- 蛋白(たんばく)質
UpToDate Contents
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English Journal
- Yeast endocytic adaptor ap-2 binds the stress sensor mid2 and functions in polarized cell responses.
- Chapa-Y-Lazo B1, Allwood EG, Smaczynska-de Rooij II, Snape ML, Ayscough KR.Author information 1Department of Biomedical Science, University of Sheffield, Sheffield, S10 2TN, UK.AbstractThe AP-2 complex is a heterotetrameric endocytic cargo-binding adaptor that facilitates uptake of membrane proteins during mammalian clathrin-mediated endocytosis. While budding yeast has clear homologues of all four AP-2 subunits which form a complex and localize to endocytic sites in vivo, the function of yeast AP-2 has remained enigmatic. Here, we demonstrate that AP-2 is required for hyphal growth in Candida albicans and polarized cell responses in Saccharomyces cerevisiae. Deletion of APM4, the cargo-binding mu subunit of AP-2, causes defects in pseudohyphal growth, generation of a mating projection and the cell wall damage response. In an apm4 null mutant, the cell wall stress sensor Mid2 is unable to relocalize to the tip of a mating projection following pheromone addition, or to the mother bud neck in response to cell wall damage. A direct binding interaction between Mid2 and the mu homology domain of Apm4 further supports a model in which AP-2 binds Mid2 to facilitate its internalization and relocalization in response to specific signals. Thus, Mid2 is the first cargo for AP-2 identified in yeast. We propose that endocytic recycling of Mid2 and other components is required for polarized cell responses ensuring cell wall deposition and is tightly monitored during cell growth.
- Traffic (Copenhagen, Denmark).Traffic.2014 May;15(5):546-57. doi: 10.1111/tra.12155. Epub 2014 Feb 25.
- The AP-2 complex is a heterotetrameric endocytic cargo-binding adaptor that facilitates uptake of membrane proteins during mammalian clathrin-mediated endocytosis. While budding yeast has clear homologues of all four AP-2 subunits which form a complex and localize to endocytic sites in vivo, the fun
- PMID 24460703
- Shank2 mutant mice display a hypersecretory response to cholera toxin.
- Jung ES1, Park J, Gee HY, Jung J, Noh SH, Lee JS, Richter W, Namkung W, Lee MG.Author information 1Department of Pharmacology, Yonsei University College of Medicine, 134 Sinchon-Dong, Seoul 120-752, Korea. mlee@yuhs.ac.AbstractShank2 is a PDZ (PSD-95/discs large/ZO-1)-based adaptor that has been suggested to regulate membrane transporting proteins in the brain and epithelial tissues. Here, we report that Shank2 mutant (Shank2(-/-)) mice exhibit aberrant fluid and ion transport in the intestine. Molecular characterization using epithelial tissues from Shank2(+/+) and Shank2(-/-) mice revealed that a long spliceoform of Shank2 (Shank2E) is predominantly expressed in the pancreatic, renal and intestinal epithelia. In functional assays, deletion of Shank2 increased the cystic fibrosis transmembrane conductance regulator (CFTR)-dependent short-circuit currents by 84% (P < 0.05) and 101% (P < 0.05) in the mouse colon and rectum, respectively. Disruption of the CFTR-Shank2-phosphodiesterase 4D protein complex appeared to be mostly responsible for the changes in CFTR activities. Notably, Shank2 deletion profoundly increased cholera toxin-induced fluid accumulation in the mouse intestine (∼90%, P < 0.01). Analyses with chemical inhibitors confirmed that the hyperactivation of CFTR channel function is responsible for the increased response to cholera toxin. These results suggest that Shank2 is a key molecule that participates in epithelial homeostasis, in particular to prevent overt secretory responses caused by epithelial pathogens.
- The Journal of physiology.J Physiol.2014 Apr 15;592(Pt 8):1809-21. doi: 10.1113/jphysiol.2013.268631. Epub 2014 Jan 20.
- Shank2 is a PDZ (PSD-95/discs large/ZO-1)-based adaptor that has been suggested to regulate membrane transporting proteins in the brain and epithelial tissues. Here, we report that Shank2 mutant (Shank2(-/-)) mice exhibit aberrant fluid and ion transport in the intestine. Molecular characterization
- PMID 24445315
- Codon Arg15 Mutations of the AP2S1 Gene: Common Occurrence in Familial Hypocalciuric Hypercalcemia Cases Negative for Calcium-sensing Receptor (CASR) Mutations.
- Hendy GN1, Canaff L, Newfield RS, Tripto-Shkolnik L, Wong BY, Lee BS, Cole DE.Author information 1Departments of Medicine, Physiology, and Human Genetics (G.N.H., L.C.), McGill University, and Calcium Research Laboratory and Hormones and Cancer Research Unit, Royal Victoria Hospital, Montreal, QC, Canada H3A 1A1; Department of Pediatrics (R.S.N.), University of California San Diego and Rady Children's Hospital San Diego, San Diego, CA 92123, USA; Diabetes and Endocrinology Unit (L.T.S.), Hillel Yaffe Medical Center, Hadera 38100, Israel; and Departments of Laboratory Medicine and Pathobiology, Medicine, and Genetics (B.Y.L.W, B.S.P.L., D.E.C.C.), University of Toronto, Toronto, ON, Canada M4N 3M5.AbstractContext: Familial hypocalciuric hypercalcemia (FHH) is an autosomal dominant disorder with three known subtypes: FHH1, FHH2, and FHH3. About 65% of FHH cases are FHH1, caused by inactivating mutations of the calcium-sensing receptor (CASR) gene. FHH3 was recently found to be caused by codon Arg15 (p.R15) mutations in the adaptor-related protein complex 2, sigma-2 subunit that interacts with the CaSR, and is encoded by the AP2S1 gene. Objective: To assess the prevalence of AP2S1 mutations, and describe the phenotype of FHH3, in an independent cohort of FHH subjects lacking CASR mutations. Patients and Methods: Thirty-nine patients presenting with some combination of hypercalcemia, hypermagnesemia, non-suppressed serum PTH levels, and reduced urinary calcium excretion were studied. Exon 2 of the AP2S1 gene was PCR amplified from patient genomic DNA and Sanger sequenced. The presence of p.R15 mutations was confirmed by restriction enzyme analysis. Results: Five of the 39 subjects had AP2S1 p.R15 mutations - a frequency of 13%. The three recurrent mutations reported previously were all found in our cohort (p.R15C in 2, p.R15L in 2, and p.R15H in one subject). The FHH3 phenotype did not differ materially from that of FHH1 due to CASR mutations. Conclusions: The results affirm that a significant number of patients suspected of having FHH but proven negative for CASR mutation have AP2S1 p.R15 mutations. Screening for AP2S1 p.R15 mutations in such cases should be considered, given the clinical benefits (avoiding unnecessary parathyroidectomy) that have already been demonstrated for CASR screening in FHH1.
- The Journal of clinical endocrinology and metabolism.J Clin Endocrinol Metab.2014 Apr 14:jc20141120. [Epub ahead of print]
- Context: Familial hypocalciuric hypercalcemia (FHH) is an autosomal dominant disorder with three known subtypes: FHH1, FHH2, and FHH3. About 65% of FHH cases are FHH1, caused by inactivating mutations of the calcium-sensing receptor (CASR) gene. FHH3 was recently found to be caused by codon Arg15 (p
- PMID 24731014
Japanese Journal
- 斎藤 潤
- 日本臨床免疫学会会誌 = Japanese journal of clinical immunology 34(1), 20-28, 2011-02-28
- 炎症反応は生体防御において極めて重要な反応であるが，過剰な炎症性応答は組織障害を引き起こす．IL-1βは主要な炎症性サイトカインの一つであり，様々な疾患がIL-1βによって惹起されることが知られている．IL-1βは前駆型のproIL-1βがインフラマソーム（inflammasome）と呼ばれるタンパク複合体により活性型に変換され，細胞外へ分泌される．インフラマソームは刺激を …
- NAID 10029431634
- 酸化ストレスセンサー Keap1 と選択的オートファジー基質p62複合体の結晶構造解析
- 黒河 博文
- 日本結晶学会誌 52(5), 250-254, 2010-10-31
- … Keap1, an adaptor protein of cullin-RING ubiquitin ligase complex, represses cytoprotective transcription factor Nrf2 in an oxidative stress-dependent manner. … Crystal structure of Keap1-p62 complex revealed the structural basis for the Nrf2 activation in which Keap1 is inactivated by p62. …
- NAID 10027673083
Related Links
- 26 Mar 2012: Hirst J, D. Barlow L, Francisco GC, Sahlender DA, Seaman MNJ, et al. (2012) Correction: The Fifth Adaptor Protein Complex. PLoS Biol 10(3): 10.1371/annotation/89dff893-c156-44bb-a731 ...
- AP3B1 A gene on chromosome 5q14.1 that encodes a subunit of the heterotetrameric AP3 complex, a protein complex composed of two large subunits (delta and beta), a medium subunit (mu), and a small subunit (sigma). AP3 ...
★リンクテーブル★
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- 英
- adaptor protein complex
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- 関
- alpha-adaptin
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アダプタータンパク質複合体サブユニット
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アダプタータンパク質複合体1
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アダプタータンパク質複合体3
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- 関
- complexes、complicated、composite、conjugate、intricate
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- 関
- accommodate、accommodation、adaptation、adaptive、orientate
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アダプタータンパク質、アダプター蛋白質、アダプタータンパク、アダプター蛋白
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- 関
- hybrid、mixed lineage、mixed type、mixed-type
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- 関
- adapter