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Integrin beta 1

From Wikipedia, the free encyclopedia
Mammalian protein found in Homo sapiens

ITGB1
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

4WK4,3G9W,3T9K,3VI3,3VI4,4DX9,4WJK,4WK0,4WK2

Identifiers
AliasesITGB1, CD29, FNRB, GPIIA, MDF2, MSK12, VLA-BETA, VLAB, integrin subunit beta 1
External IDsOMIM:135630;MGI:96610;HomoloGene:22999;GeneCards:ITGB1;OMA:ITGB1 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for ITGB1
Genomic location for ITGB1
Band10p11.22Start32,900,319bp[1]
End33,005,792bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for ITGB1
Genomic location for ITGB1
Band8|8 E2Start129,412,135bp[2]
End129,459,681bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • visceral pleura

  • seminal vesicula

  • tail of epididymis

  • parietal pleura

  • stromal cell of endometrium

  • tibia

  • smooth muscle tissue

  • superficial temporal artery

  • Descending thoracic aorta

  • palpebral conjunctiva
Top expressed in
  • Ileal epithelium

  • stroma of bone marrow

  • lactiferous gland

  • left lung lobe

  • cardiac muscle tissue of left ventricle

  • umbilical cord

  • atrium

  • uterus

  • calvaria

  • extraocular muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3688

16412

Ensembl

ENSG00000150093

ENSMUSG00000025809

UniProt

P05556

P09055

RefSeq (mRNA)
NM_002211
NM_033666
NM_033667
NM_033668
NM_033669

NM_133376

NM_010578

RefSeq (protein)

NP_002202
NP_391988
NP_596867

NP_034708

Location (UCSC)Chr 10: 32.9 – 33.01 MbChr 8: 129.41 – 129.46 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Integrin beta-1 (ITGB1), also known asCD29, is acell surface receptor that in humans is encoded by theITGB1gene.[5] Thisintegrin associates withintegrin alpha 1 andintegrin alpha 2 to form integrin complexes which function ascollagen receptors. It also forms dimers withintegrin alpha 3 to form integrin receptors fornetrin 1 andreelin. These and other integrin beta 1 complexes have been historically known as very late activation (VLA) antigens.

Integrin beta 1 is expressed as at least four differentisoforms. Incardiac muscle andskeletal muscle, the integrin beta-1D isoform is specifically expressed, and localizes tocostameres, where it aids in the lateral force transmission from theZ-discs to theextracellular matrix. Abnormal levels of integrin beta-1D have been found inlimb girdle muscular dystrophy andpolyneuropathy.

Structure

[edit]

Integrin beta-1 can exist as differentisoforms viaalternative splicing. Sixalternatively spliced variants have been found for this gene which encode five proteins with alternateC-termini.[6] Integrin receptors exist as heterodimers, and greater than 20 different integrin heterodimeric receptors have been described. All integrins, alpha and beta forms, have large extracellular and short intracellular domains.[7] The cytoplasmic domain of integrin beta-1 binds to theactincytoskeleton.[8] Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.[7]

Function

[edit]

Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis,hemostasis, tissue repair,immune response andmetastatic diffusion of tumor cells.[7] Integrins link theactincytoskeleton with theextracellular matrix and they transmit signals bidirectionally between theextracellular matrix andcytoplasmic domains.[9][10]Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainlyfocal adhesions.[8][11] Integrin beta-1 mutants lose the ability to target to sites offocal adhesions.[12][13]

Three novel isoforms of integrin beta-1 have been identified, termed beta-1B, beta-1C and beta-1D. Integrin beta-1B is transcribed when the proximal 26amino acids of thecytoplasmic domain in exon 6 are retained and then succeeded by a 12amino acid stretch from an adjacentintronic region.[14] The integrin beta-1Bisoform appears to act as a dominant negative in that it inhibits cell adhesion.[15] A second integrin beta-1isoform, termed beta-1C, was described to have an additional 48amino acids appended to the 26amino acids in thecytoplasmic domain;[16] the function of this isoform was an inhibitory one onDNA synthesis in theG1 phase of thecell cycle.[17] The thirdisoform, termed beta-1D, is astriated muscle-specific isoform, which replaces the canonical beta-1Aisoform incardiac andskeletal muscle cells. Thisisoform is produced from splicing into a novel additional exon between exons 6 and 7. Thecytoplasmic domain of integrin beta-1D replaces the distal 21amino acids (present in integrin beta-1A) with an alternative stretch of 24amino acids (13 unique).[18][19]

Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,[19] appearing immediately following the fusion ofmyoblasts inC2C12 cell with rising levels throughoutmyofibrillar differentiation.[20] Integrin beta-1D is specifically localized tocostameres andintercalated discs ofcardiac muscle andcostameres,myotendinous junctions andneuromuscular junctions ofskeletal muscle, and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface ofCHO cells resulted intyrosinephosphorylation ofpp125FAK and inducedmitogen-activated protein kinase activation.[20]

Clinical significance

[edit]

In patients withlimb girdle muscular dystrophy, type 2C, beta-1D integrin has been shown to be severely reduced inskeletal muscle biopsies, coordinate with a reduction inalpha 7B-integrin andfilamin 2.[21]

In patients with sensitive-motorpolyneuropathy, levels ofintegrin alpha-7B, integrin beta-1D andagrin were significantly reduced nearly to undetectable levels; and this corresponded with lowermRNA levels.[22]

Interactions

[edit]

CD29 has been shown tointeract with

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000150093 –Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000025809 –Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Goodfellow PJ, Nevanlinna HA, Gorman P, Sheer D, Lam G, Goodfellow PN (Jan 1989). "Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2".Annals of Human Genetics.53 (Pt 1):15–22.doi:10.1111/j.1469-1809.1989.tb01118.x.PMID 2524991.S2CID 36485270.
  6. ^"Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)".
  7. ^abcHynes RO (Apr 1992). "Integrins: versatility, modulation, and signaling in cell adhesion".Cell.69 (1):11–25.doi:10.1016/0092-8674(92)90115-s.PMID 1555235.S2CID 32774108.
  8. ^abSastry SK, Horwitz AF (Oct 1993). "Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling".Current Opinion in Cell Biology.5 (5):819–31.doi:10.1016/0955-0674(93)90031-k.PMID 8240826.
  9. ^Burridge K, Chrzanowska-Wodnicka M (1996)."Focal adhesions, contractility, and signaling".Annual Review of Cell and Developmental Biology.12:463–518.doi:10.1146/annurev.cellbio.12.1.463.PMID 8970735.S2CID 28558568.
  10. ^Schwartz MA, Schaller MD, Ginsberg MH (1995). "Integrins: emerging paradigms of signal transduction".Annual Review of Cell and Developmental Biology.11:549–99.doi:10.1146/annurev.cb.11.110195.003001.PMID 8689569.
  11. ^LaFlamme SE, Akiyama SK, Yamada KM (Apr 1992)."Regulation of fibronectin receptor distribution".The Journal of Cell Biology.117 (2):437–47.doi:10.1083/jcb.117.2.437.PMC 2289425.PMID 1373145.
  12. ^Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE (Jun 1994)."Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras".The Journal of Biological Chemistry.269 (23):15961–4.doi:10.1016/S0021-9258(17)33955-8.PMID 7515874.
  13. ^Reszka AA, Hayashi Y, Horwitz AF (Jun 1992)."Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association".The Journal of Cell Biology.117 (6):1321–30.doi:10.1083/jcb.117.6.1321.PMC 2289496.PMID 1376731.
  14. ^Altruda F, Cervella P, Tarone G, Botta C, Balzac F, Stefanuto G, Silengo L (Nov 1990). "A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing".Gene.95 (2):261–6.doi:10.1016/0378-1119(90)90369-3.PMID 2249781.
  15. ^Balzac F, Retta SF, Albini A, Melchiorri A, Koteliansky VE, Geuna M, Silengo L, Tarone G (Oct 1994)."Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility".The Journal of Cell Biology.127 (2):557–65.doi:10.1083/jcb.127.2.557.hdl:2318/39410.PMC 2120206.PMID 7523423.
  16. ^Languino LR, Ruoslahti E (Apr 1992)."An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain".The Journal of Biological Chemistry.267 (10):7116–20.doi:10.1016/S0021-9258(19)50545-2.PMID 1551917.
  17. ^Meredith J, Takada Y, Fornaro M, Languino LR, Schwartz MA (Sep 1995). "Inhibition of cell cycle progression by the alternatively spliced integrin beta 1C".Science.269 (5230):1570–2.Bibcode:1995Sci...269.1570M.doi:10.1126/science.7545312.PMID 7545312.
  18. ^Zhidkova NI, Belkin AM, Mayne R (Sep 1995). "Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle".Biochemical and Biophysical Research Communications.214 (1):279–85.Bibcode:1995BBRC..214..279Z.doi:10.1006/bbrc.1995.2285.PMID 7545396.
  19. ^abvan der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A (Aug 1995)."A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle".FEBS Letters.369 (2–3):340–4.Bibcode:1995FEBSL.369..340V.doi:10.1016/0014-5793(95)00814-p.PMID 7544298.S2CID 86638879.
  20. ^abBelkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K (Jan 1996)."Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells".The Journal of Cell Biology.132 (1–2):211–26.doi:10.1083/jcb.132.1.211.PMC 2120711.PMID 8567725.
  21. ^Anastasi G, Cutroneo G, Trimarchi F, Santoro G, Bruschetta D, Bramanti P, Pisani A, Favaloro A (Dec 2004). "Evaluation of sarcoglycans, vinculin-talin-integrin system and filamin2 in alpha- and gamma-sarcoglycanopathy: an immunohistochemical study".International Journal of Molecular Medicine.14 (6):989–99.doi:10.3892/ijmm.14.6.989.PMID 15547664.
  22. ^Anastasi G, Cutroneo G, Santoro G, Arco A, Rizzo G, Bramanti P, Rinaldi C, Sidoti A, Amato A, Favaloro A (Sep 2008)."Costameric proteins in human skeletal muscle during muscular inactivity".Journal of Anatomy.213 (3):284–95.doi:10.1111/j.1469-7580.2008.00921.x.PMC 2732038.PMID 18537849.
  23. ^Otey CA, Pavalko FM, Burridge K (Aug 1990)."An interaction between alpha-actinin and the beta 1 integrin subunit in vitro".The Journal of Cell Biology.111 (2):721–9.doi:10.1083/jcb.111.2.721.PMC 2116186.PMID 2116421.
  24. ^Otey CA, Vasquez GB, Burridge K, Erickson BW (Oct 1993)."Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain".The Journal of Biological Chemistry.268 (28):21193–7.doi:10.1016/S0021-9258(19)36909-1.PMID 7691808.
  25. ^Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E (Mar 2000)."CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans".European Journal of Immunology.30 (3):900–7.doi:10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X.PMID 10741407.
  26. ^Radford KJ, Thorne RF, Hersey P (May 1996). "CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma".Biochemical and Biophysical Research Communications.222 (1):13–8.Bibcode:1996BBRC..222...13R.doi:10.1006/bbrc.1996.0690.PMID 8630057.
  27. ^abMazzocca A, Carloni V, Sciammetta S, Cordella C, Pantaleo P, Caldini A, Gentilini P, Pinzani M (Sep 2002). "Expression of transmembrane 4 superfamily (TM4SF) proteins and their role in hepatic stellate cell motility and wound healing migration".Journal of Hepatology.37 (3):322–30.doi:10.1016/S0168-8278(02)00175-7.PMID 12175627.
  28. ^Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M (Oct 2000)."The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes".The Journal of Biological Chemistry.275 (43):33669–78.doi:10.1074/jbc.M002519200.PMID 10906324.
  29. ^abvan der Flier A, Kuikman I, Kramer D, Geerts D, Kreft M, Takafuta T, Shapiro SS, Sonnenberg A (Jan 2002)."Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits".The Journal of Cell Biology.156 (2):361–76.doi:10.1083/jcb.200103037.PMC 2199218.PMID 11807098.
  30. ^Loo DT, Kanner SB, Aruffo A (Sep 1998)."Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction".The Journal of Biological Chemistry.273 (36):23304–12.doi:10.1074/jbc.273.36.23304.PMID 9722563.
  31. ^Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E (May 1999)."Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions".The Biochemical Journal.340 (Pt 1):103–11.doi:10.1042/0264-6021:3400103.PMC 1220227.PMID 10229664.
  32. ^abLee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM (Nov 2002)."Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction".Osteoarthritis and Cartilage.10 (11):890–7.doi:10.1053/joca.2002.0842.PMID 12435334.
  33. ^Liliental J, Chang DD (Jan 1998)."Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit".The Journal of Biological Chemistry.273 (4):2379–83.doi:10.1074/jbc.273.4.2379.PMID 9442085.
  34. ^Chang DD, Wong C, Smith H, Liu J (Sep 1997)."ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin".The Journal of Cell Biology.138 (5):1149–57.doi:10.1083/jcb.138.5.1149.PMC 2136751.PMID 9281591.
  35. ^Chang DD, Hoang BQ, Liu J, Springer TA (Mar 2002)."Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin".The Journal of Biological Chemistry.277 (10):8140–5.doi:10.1074/jbc.M109031200.PMID 11741908.
  36. ^Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (Jul 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis".Journal of Cell Science.113 (13):2385–97.doi:10.1242/jcs.113.13.2385.PMID 10852818.
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  38. ^Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C (Jun 2002)."Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement".The Journal of Biological Chemistry.277 (23):20895–902.doi:10.1074/jbc.M200200200.PMID 11919189.
  39. ^Parsons M, Keppler MD, Kline A, Messent A, Humphries MJ, Gilchrist R, Hart IR, Quittau-Prevostel C, Hughes WE, Parker PJ, Ng T (Aug 2002)."Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis".Molecular and Cellular Biology.22 (16):5897–911.doi:10.1128/MCB.22.16.5897-5911.2002.PMC 133968.PMID 12138200.
  40. ^Tapley P, Horwitz A, Buck C, Duggan K, Rohrschneider L (Mar 1989). "Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts".Oncogene.4 (3):325–33.PMID 2468126.
  41. ^Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K (1986)."Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage".Nature.320 (6062):531–3.Bibcode:1986Natur.320..531H.doi:10.1038/320531a0.PMID 2938015.S2CID 4356748.
  42. ^Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (Nov 1997)."NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins".The Journal of Biological Chemistry.272 (46):29181–9.doi:10.1074/jbc.272.46.29181.PMID 9360996.
  43. ^Han DC, Rodriguez LG, Guan JL (Jan 2001). "Identification of a novel interaction between integrin beta1 and 14-3-3beta".Oncogene.20 (3):346–57.doi:10.1038/sj.onc.1204068.PMID 11313964.S2CID 7405925.

Further reading

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External links

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Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:
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