アンキリン
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/24 11:30:07」(JST)
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| ANK1, erythrocytic |
|
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.[1]
|
| Identifiers |
| Symbol |
ANK1 |
| Alt. symbols |
AnkyrinR, Band2.1 |
| Entrez |
286 |
| HUGO |
492 |
| OMIM |
182900 |
| PDB |
1N11 |
| RefSeq |
NM_000037 |
| UniProt |
P16157 |
| Other data |
| Locus |
Chr. 8 p21.1-11.2 |
| Ankyrin repeat |
| Identifiers |
| Symbol |
Ank |
| Pfam |
PF00023 |
| InterPro |
IPR002110 |
| SMART |
SM00248 |
| PROSITE |
PDOC50088 |
| SCOP |
1awc |
| SUPERFAMILY |
1awc |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
| ANK2, neuronal |
| Identifiers |
| Symbol |
ANK2 |
| Alt. symbols |
AnkyrinB |
| Entrez |
287 |
| HUGO |
493 |
| OMIM |
106410 |
| RefSeq |
NM_001148 |
| UniProt |
Q01484 |
| Other data |
| Locus |
Chr. 4 q25-q27 |
| ANK3, node of Ranvier |
| Identifiers |
| Symbol |
ANK3 |
| Alt. symbols |
AnkyrinG |
| Entrez |
288 |
| HUGO |
494 |
| OMIM |
600465 |
| RefSeq |
NM_020987 |
| UniProt |
Q12955 |
| Other data |
| Locus |
Chr. 10 q21 |
Ankyrins are a family of adaptor proteins that mediate the attachment of integral membrane proteins to the spectrin-actin based membrane cytoskeleton.[2] Ankyrins have binding sites for the beta subunit of spectrin and at least 12 families of integral membrane proteins. This linkage is required to maintain the integrity of the plasma membranes and to anchor specific ion channels, ion exchangers and ion transporters in the plasma membrane. The name is derived from the Greek word for "fused".
Contents
- 1 Structure
- 2 Subtypes
- 2.1 ANK1
- 2.2 ANK2
- 2.3 ANK3
- 3 See also
- 4 References
- 5 External links
Structure
Ankyrins contain four functional domains: an N-terminal domain that contains 24 tandem ankyrin repeats, a central domain that binds to spectrin, a death domain that binds to proteins involved in apoptosis, and a C-terminal regulatory domain that is highly variable between different ankyrin proteins.[2]
Subtypes
Ankyrins are encoded by three genes (ANK1, ANK2 and ANK3) in mammals. Each gene in turn produces multiple proteins through alternative splicing.
ANK1
The ANK1 gene encodes the AnkyrinR proteins. AnkyrinR was first characterized in human erythrocytes, where this ankyrin was referred to as erythrocyte ankyrin or band2.1.[3] AnkyrinR enables erythrocytes to resist shear forces experienced in the circulation. Individuals with reduced or defective ankyrinR have a form of hemolytic anemia termed hereditary spherocytosis.[4] In erythrocytes, AnkyrinR links the membrane skeleton to the Cl−/HCO3− anion exchanger.[5]
Ankyrin 1 links membrane receptor CD44 to the inositol triphosphate receptor and the cytoskeleton.[6]
It has been suggested that Ankyrin 1 interacts with KAHRP (shown via selective pull-downs, SPR and ELISA).[7]
ANK2
Subsequently, ankyrinB proteins (products of the ANK2 gene[8]) were identified in brain and muscle. AnkyrinB and AnkyrinG proteins are required for the polarized distribution of many membrane proteins including the Na+/K+ ATPase, the voltage gated Na+ channel and the Na+/Ca2+ exchanger.
ANK3
AnkyrinG proteins (products of the ANK3 gene[9]) were identified in epithelial cells and neurons. A large-scale genetic analysis conducted in 2008 shows the possibility that ANK3 is involved in bipolar disorder.[10][11]
See also
- DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats
References
- ^ PDB: 1N11; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ankyrinR". EMBO J. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
- ^ a b Bennett V, Baines AJ (1 July 2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiol. Rev. 81 (3): 1353–92. PMID 11427698.
- ^ Bennett V, Stenbuck PJ (10 April 1979). "Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin". J Biol Chem 254 (7): 2533–41. PMID 372182.
- ^ Lux SE, Tse WT, Menninger JC, John KM, Harris P, Shalev O, Chilcote RR, Marchesi SL, Watkins PC, Bennett V (1990). "Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8". Nature 345 (6277): 736–9. doi:10.1038/345736a0. PMID 2141669.
- ^ Bennett V, Stenbuck PJ (1979). "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes". Nature 280 (5722): 468–73. doi:10.1038/280468a0. PMID 379653.
- ^ Singleton PA, Bourguignon LY (2004). "CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation". Exp Cell Res 295 (1): 102–18. doi:10.1016/j.yexcr.2003.12.025. PMID 15051494.
- ^ Weng, H; Guo, X; Papoin, J; Wang, J; Coppel, R; Mohandas, N; An, X (2014). "Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane". Biochimica et Biophysica Acta (BBA) - Biomembranes 1838 (1 Pt B): 185–92. doi:10.1016/j.bbamem.2013.09.014. PMID 24090929.
- ^ Schott JJ, Charpentier F, Peltier S; et al. (November 1995). "Mapping of a Gene for Long QT Syndrome to Chromosome 4q25-27". Am. J. Hum. Genet. 57 (5): 1114–22. PMC 1801360. PMID 7485162.
- ^ Kapfhamer D, Miller DE, Lambert S, Bennett V, Glover TW, Burmeister M (May 1995). "Chromosomal localization of the ankyrinG gene (ANK3/Ank3) to human 10q21 and mouse 10". Genomics 27 (1): 189–91. doi:10.1006/geno.1995.1023. PMID 7665168.
- ^ Ferreira MA, O'Donovan MC, Meng YA; et al. (August 2008). "Collaborative genome-wide association analysis supports a role for ANK3 and CACNA1C in bipolar disorder". Nat. Genet. 40 (9): 1056–8. doi:10.1038/ng.209. PMC 2703780. PMID 18711365.
- ^ "Channeling Mental Illness: GWAS Links Ion Channels, Bipolar Disorder". Schizophrenia Research Forum: News. schizophreniaforum.org. 2008-08-19. Retrieved 2008-08-21.
External links
- Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH)
- Proteopedia 1n11 Ankyrin-R
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Proteins of the cytoskeleton
|
|
| Human |
|
|
| Nonhuman |
- Major sperm proteins
- Prokaryotic cytoskeleton
|
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See also: cytoskeletal defects
|
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UpToDate Contents
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English Journal
- Analysis of ANKKI (rs1800497) and DRD2 (rs1079597, rs1800498) variants in five ethnic groups from Punjab, North-West India.
- Singh G1, Talwar I2, Sharma R3, Sandhu HS3, Matharoo K4, Bhanwer AJ5.
- Gene.Gene.2016 Jun 10;584(1):69-74. doi: 10.1016/j.gene.2016.03.009. Epub 2016 Mar 10.
- Dopamine D2 receptor (DRD2) is one of the essential neurotransmitters in the brain studied extensively in the field of psychiatric disorders, alcoholic behaviors and Pharmacology. It is also a promising gene for studying the evolutionary and genetic variation among populations. The present study was
- PMID 26970175
- A novel 3-(4,5-diphenyl-1,3-oxazol-2-yl)propanal oxime compound is a potent Transient Receptor Potential Ankyrin 1 and Vanilloid 1 (TRPA1 and V1) receptor antagonist.
- Payrits M1, Sághy É2, Mátyus P3, Czompa A4, Ludmerczki R5, Deme R6, Sándor Z7, Helyes Z8, Szőke É9.
- Neuroscience.Neuroscience.2016 Jun 2;324:151-62. doi: 10.1016/j.neuroscience.2016.02.049. Epub 2016 Feb 27.
- Transient Receptor Potential Ankyrin 1 and Vanilloid 1 (TRPA1, TRPV1) ion channels expressed on nociceptive primary sensory neurons are important regulators of pain and inflammation. TRPA1 is activated by several inflammatory mediators including formaldehyde and methylglyoxal that are products of th
- PMID 26930003
- Hydroxychloroquine binding to cytoplasmic domain of Band 3 in human erythrocytes: Novel mechanistic insights into drug structure, efficacy and toxicity.
- Nakagawa M1, Sugawara K2, Goto T1, Wakui H1, Nunomura W3.
- Biochemical and biophysical research communications.Biochem Biophys Res Commun.2016 May 13;473(4):999-1004. doi: 10.1016/j.bbrc.2016.04.005. Epub 2016 Apr 2.
- Hydroxychloroquine (HCQ) is a widely used drug in the treatment of autoimmune diseases, such as arthritis and systemic lupus erythematosus. It has also been prescribed for the treatment of malaria owing to its lower toxicity compared to its closely related compound chloroquine (CQ). However, the mec
- PMID 27049308
Japanese Journal
- ankAT-1 is a novel gene mediating the apical tuft formation in the sea urchin embryo
- Yaguchi Shunsuke,Yaguchi Junko,Wei Zheng,Shiba Kogiku,Angerer Lynne M.,Inaba Kazuo,谷口 俊介,柴 小菊,稲葉 一男
- Developmental biology 348(1), 67-75, 2010-12
- … The most strongly down-regulated gene in FoxQ2 morphants encodes a protein with ankyrin repeats region in its N-terminal domain. … We named this gene ankAT-1, Ankyrin-containing gene specific for Apical Tuft. …
- NAID 120002808047
- The forced aggresome formation of a bovine anion exchanger 1 (AE1) mutant through association with ΔF508-cystic fibrosis transmembrane conductance regulator upon proteasome inhibition in HEK293 cells
- Adachi Hirokazu,Kurooka Takao,Otsu Wataru,Inaba Mutsumi
- Japanese Journal of Veterinary Research 58(2), 101-110, 2010-08
- … R664X AE1 and EGFP-ΔF508-CFTRshowed co-localization in the aggregates and signals of which coincided with γ-tubulin and were caged by vimentin at the pericentriolar locus, demonstrating aggresome formation.On the other hand, EGFP-AnkN90, consisting of the N-terminal AE1 binding domain of ankyrin, a ytoplasmic protein, also exhibited co-localization with R664X AE1, but was found throughout the ER. …
- NAID 120002261730
Related Links
- ankyrin 【名】《化学》アンキリン - アルクがお届けする進化するオンライン英和・和英辞書データベース。一般的な単語や連語から、イディオム、専門用語、スラングまで幅広く収録。 ... 英和・和英 対訳データオンライン検索サービス
- Current views of ankyrin function are based on co-localization and biochemical interactions of ankyrin with other proteins. Ankyrin associates with a variety of membrane proteins including ion ...
Related Pictures
★リンクテーブル★
[★]
- 英
- ankyrin
- 関
- スペクトリン、バンド3蛋白
[★]
アンキリンリピート、アンキリン反復配列、ANKリピート
- 関
- ANK repeat、ankyrin-like repeat
[★]
アンキリン欠損
- 関
- アンキリン