“ANK1”的意思、由来-开放百科全书

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

1. ^{{cite journal | vauthors = Lambert S, Yu H, Prchal JT | title = cDNA sequence for human erythrocyte ankyrin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 5 | pages = 1730–4 |date=March 1990 | pmid = 1689849 | pmc = 53556 | doi = 10.1073/pnas.87.5.1730| url = http://www.pnas.org/content/87/5/1730.abstract | issn = |display-authors=etal| bibcode = 1990PNAS...87.1730L }}
2. ^¹²³⁴{{cite web | title = Entrez Gene: ANK1 ankyrin 1, erythrocytic| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=286| accessdate = }}
3. ^{{Cite journal | pmid = 25129075| year = 2014| author1 = De Jager| first1 = P. L.| title = Alzheimer's disease: Early alterations in brain DNA methylation at ANK1, BIN1, RHBDF2 and other loci| journal = Nature Neuroscience| volume = 17| issue = 9| pages = 1156–63| last2 = Srivastava| first2 = G| last3 = Lunnon| first3 = K| last4 = Burgess| first4 = J| last5 = Schalkwyk| first5 = L. C.| last6 = Yu| first6 = L| last7 = Eaton| first7 = M. L.| last8 = Keenan| first8 = B. T.| last9 = Ernst| first9 = J| last10 = McCabe| first10 = C| last11 = Tang| first11 = A| last12 = Raj| first12 = T| last13 = Replogle| first13 = J| last14 = Brodeur| first14 = W| last15 = Gabriel| first15 = S| last16 = Chai| first16 = H. S.| last17 = Younkin| first17 = C| last18 = Younkin| first18 = S. G.| last19 = Zou| first19 = F| last20 = Szyf| first20 = M| last21 = Epstein| first21 = C. B.| last22 = Schneider| first22 = J. A.| last23 = Bernstein| first23 = B. E.| last24 = Meissner| first24 = A| last25 = Ertekin-Taner| first25 = N| last26 = Chibnik| first26 = L. B.| last27 = Kellis| first27 = M| last28 = Mill| first28 = J| last29 = Bennett| first29 = D. A.| doi = 10.1038/nn.3786 | pmc=4292795}}
4. ^{{Cite journal | pmid = 25129077| year = 2014| author1 = Lunnon| first1 = K| title = Methylomic profiling implicates cortical deregulation of ANK1 in Alzheimer's disease| journal = Nature Neuroscience| volume = 17| issue = 9| pages = 1164–70| last2 = Smith| first2 = R| last3 = Hannon| first3 = E| last4 = De Jager| first4 = P. L.| last5 = Srivastava| first5 = G| last6 = Volta| first6 = M| last7 = Troakes| first7 = C| last8 = Al-Sarraj| first8 = S| last9 = Burrage| first9 = J| last10 = MacDonald| first10 = R| last11 = Condliffe| first11 = D| last12 = Harries| first12 = L. W.| last13 = Katsel| first13 = P| last14 = Haroutunian| first14 = V| last15 = Kaminsky| first15 = Z| last16 = Joachim| first16 = C| last17 = Powell| first17 = J| last18 = Lovestone| first18 = S| last19 = Bennett| first19 = D. A.| last20 = Schalkwyk| first20 = L. C.| last21 = Mill| first21 = J| doi = 10.1038/nn.3782 | pmc=4410018}}
5. ^{{Cite journal | pmid = 25493648| pmc = 4262449| year = 2014| author1 = Liscovitch| first1 = N| title = Differential Co-Expression between α-Synuclein and IFN-γ Signaling Genes across Development and in Parkinson's Disease| journal = PLoS ONE| volume = 9| issue = 12| pages = e115029| last2 = French| first2 = L| doi = 10.1371/journal.pone.0115029| bibcode = 2014PLoSO...9k5029L}}
6. ^{{cite journal | vauthors = Borzok MA, Catino DH, Nicholson JD, Kontrogianni-Konstantopoulos A, Bloch RJ | title = Mapping the binding site on small ankyrin 1 for obscurin | journal = J. Biol. Chem. | volume = 282 | issue = 44 | pages = 32384–96 |date=November 2007 | pmid = 17720975 | doi = 10.1074/jbc.M704089200 | url = | issn = }}
7. ^{{cite journal |doi=10.1083/jcb.150.1.177 |last=Bourguignon |first=L Y |author2=Zhu H |author3=Shao L |author4=Chen Y W |date=July 2000 |title=Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration |journal=J. Cell Biol. |volume=150 |issue=1 |pages=177–91 | issn = 0021-9525| pmid = 10893266 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=2185563 }}
8. ^{{cite journal |last=Kontrogianni-Konstantopoulos |first=Aikaterini |author2=Bloch Robert J |date=February 2003 |title=The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin |journal=J. Biol. Chem. |volume=278 |issue=6 |pages=3985–91 | issn = 0021-9258| pmid = 12444090 |doi = 10.1074/jbc.M209012200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
9. ^{{cite journal |last=Nicolas |first=Virginie |last2=Le Van Kim |first2=Caroline |last3=Gane |first3=Pierre |last4=Birkenmeier |first4=Connie |last5=Cartron |first5=Jean-Pierre |last6=Colin |first6=Yves |last7=Mouro-Chanteloup |first7=Isabelle |date=July 2003 |title=Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation |journal=J. Biol. Chem. |volume=278 |issue=28 |pages=25526–33 | issn = 0021-9258| pmid = 12719424 |doi = 10.1074/jbc.M302816200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
10. ^{{cite journal |last=Kontrogianni-Konstantopoulos |first=Aikaterini |author2=Jones Ellene M |author3=Van Rossum Damian B |author4=Bloch Robert J |date=March 2003 |title=Obscurin is a ligand for small ankyrin 1 in skeletal muscle |journal=Mol. Biol. Cell |volume=14 |issue=3 |pages=1138–48 | issn = 1059-1524| pmid = 12631729 |doi = 10.1091/mbc.E02-07-0411 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=151585 }}

Tissue distribution