Biology:Ankyrin-1
 Generic protein structure example |
Ankyrin 1, also known as ANK-1, and erythrocyte ankyrin, is a protein that in humans is encoded by the ANK1 gene.[1][2]
Tissue distribution
The protein encoded by this gene, Ankyrin 1, is the prototype of the ankyrin family, was first discovered in erythrocytes, but since has also been found in brain and muscles.[2]
Genetics
Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known. Alternative polyadenylation accounting for the different sized erythrocytic ankyrin 1 mRNAs, has also been reported. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.[2]
Disease linkage
Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis.[2]
ANK1 shows altered methylation and expression in Alzheimer's disease.[3][4] A gene expression study of postmortem brains has suggested ANK1 interacts with interferon-γ signalling.[5]
Function
The ANK1 protein belongs to the ankyrin family that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact, and maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin-binding domain; and a carboxy-terminal regulatory domain, which is the least conserved and subject to variation.[2]
The small ANK1 (sAnk1) protein splice variants makes contacts with obscurin, a giant protein surrounding the contractile apparatus in striated muscle.[6]
Interactions
ANK1 has been shown to interact with T-cell lymphoma invasion and metastasis-inducing protein 1,[7] Titin,[8] RHAG[9] and OBSCN.[10]
See also
References
- ↑ "cDNA sequence for human erythrocyte ankyrin". Proceedings of the National Academy of Sciences of the United States of America 87 (5): 1730–1734. March 1990. doi:10.1073/pnas.87.5.1730. PMID 1689849. Bibcode: 1990PNAS...87.1730L.
- ↑ 2.0 2.1 2.2 2.3 2.4 "Entrez Gene: ANK1 ankyrin 1, erythrocytic". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=286.
- ↑ "Alzheimer's disease: early alterations in brain DNA methylation at ANK1, BIN1, RHBDF2 and other loci". Nature Neuroscience 17 (9): 1156–1163. September 2014. doi:10.1038/nn.3786. PMID 25129075.
- ↑ "Methylomic profiling implicates cortical deregulation of ANK1 in Alzheimer's disease". Nature Neuroscience 17 (9): 1164–1170. September 2014. doi:10.1038/nn.3782. PMID 25129077.
- ↑ "Differential Co-Expression between α-Synuclein and IFN-γ Signaling Genes across Development and in Parkinson's Disease". PLOS ONE 9 (12). 2014. doi:10.1371/journal.pone.0115029. PMID 25493648. Bibcode: 2014PLoSO...9k5029L.
- ↑ "Mapping the binding site on small ankyrin 1 for obscurin". The Journal of Biological Chemistry 282 (44): 32384–32396. November 2007. doi:10.1074/jbc.M704089200. PMID 17720975.
- ↑ "Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration". The Journal of Cell Biology 150 (1): 177–191. July 2000. doi:10.1083/jcb.150.1.177. PMID 10893266.
- ↑ "The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin". The Journal of Biological Chemistry 278 (6): 3985–3991. February 2003. doi:10.1074/jbc.M209012200. PMID 12444090.
- ↑ "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". The Journal of Biological Chemistry 278 (28): 25526–25533. July 2003. doi:10.1074/jbc.M302816200. PMID 12719424.
- ↑ "Obscurin is a ligand for small ankyrin 1 in skeletal muscle". Molecular Biology of the Cell 14 (3): 1138–1148. March 2003. doi:10.1091/mbc.E02-07-0411. PMID 12631729.
Further reading
- "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiological Reviews 81 (3): 1353–1392. July 2001. doi:10.1152/physrev.2001.81.3.1353. PMID 11427698.
- "Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues". Nature 281 (5732): 597–599. October 1979. doi:10.1038/281597a0. PMID 492324. Bibcode: 1979Natur.281..597B.
- "cDNA sequence for human erythrocyte ankyrin". Proceedings of the National Academy of Sciences of the United States of America 87 (5): 1730–1734. March 1990. doi:10.1073/pnas.87.5.1730. PMID 1689849. Bibcode: 1990PNAS...87.1730L.
- "Immunocytochemical localization of fodrin and ankyrin in bovine chromaffin cells in vitro". The Journal of Histochemistry and Cytochemistry 39 (11): 1485–1493. November 1991. doi:10.1177/39.11.1833445. PMID 1833445.
- "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins". Nature 344 (6261): 36–42. March 1990. doi:10.1038/344036a0. PMID 2137557. Bibcode: 1990Natur.344...36L.
- "Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin". The Journal of Biological Chemistry 265 (18): 10589–10596. June 1990. doi:10.1016/S0021-9258(18)86987-3. PMID 2141335.
- "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3". The Journal of Biological Chemistry 263 (21): 10212–10218. July 1988. doi:10.1016/S0021-9258(19)81500-4. PMID 2968981.
- "Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3". Journal of Cellular Biochemistry 37 (3): 301–315. July 1988. doi:10.1002/jcb.240370305. PMID 2970468.
- "Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin". The Journal of Biological Chemistry 263 (28): 14417–14425. October 1988. doi:10.1016/S0021-9258(18)68236-5. PMID 2971657.
- "Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles". The Journal of Biological Chemistry 255 (24): 11965–11972. December 1980. doi:10.1016/S0021-9258(19)70228-2. PMID 6449514.
- "Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction". Journal of Immunology 151 (12): 6634–6644. December 1993. doi:10.4049/jimmunol.151.12.6634. PMID 7505012.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin". Journal of Cell Science. 105 105 (4): 1137–1142. August 1993. doi:10.1242/jcs.105.4.1137. PMID 8227202.
- "The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells". The Journal of Biological Chemistry 268 (10): 7290–7297. April 1993. doi:10.1016/S0021-9258(18)53175-6. PMID 8385102.
- "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis". Nature Genetics 13 (2): 214–218. June 1996. doi:10.1038/ng0696-214. PMID 8640229.
- "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization". Genome Research 6 (1): 35–42. January 1996. doi:10.1101/gr.6.1.35. PMID 8681137.
- "Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis". British Journal of Haematology 93 (4): 828–834. June 1996. doi:10.1046/j.1365-2141.1996.d01-1746.x. PMID 8703812.
- "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle". The Journal of Cell Biology 136 (3): 621–631. February 1997. doi:10.1083/jcb.136.3.621. PMID 9024692.
- "Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing". The Journal of Biological Chemistry 272 (31): 19220–19228. August 1997. doi:10.1074/jbc.272.31.19220. PMID 9235914.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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External links
- ANK1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human ANK1 genome location and ANK1 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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