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F r o m W i k i p e d i a , t h e f r e e e n c y c l o p e d i a
( R e d i r e c t e d f r o m I T G B 1 )
Mammalian protein found in Homo sapiens
Integrin beta-1 (ITGB1 ), also known as CD29 , is a cell surface receptor that in humans is encoded by the ITGB1 gene .[5] This integrin associates with integrin alpha 1 and integrin alpha 2 to form integrin complexes which function as collagen receptors . It also forms dimers with integrin alpha 3 to form integrin receptors for netrin 1 and reelin . 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 different isoforms . In cardiac muscle and skeletal muscle , the integrin beta-1D isoform is specifically expressed, and localizes to costameres , where it aids in the lateral force transmission from the Z-discs to the extracellular matrix . Abnormal levels of integrin beta-1D have been found in limb girdle muscular dystrophy and polyneuropathy .
Structure
[ edit ]
Integrin beta-1 can exist as different isoforms via alternative splicing . Six alternatively spliced variants have been found for this gene which encode five proteins with alternate C-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 the actin cytoskeleton .[8] Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.[7]
Function
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Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis , tissue repair, immune response and metastatic diffusion of tumor cells .[7] Integrins link the actin cytoskeleton with the extracellular matrix and they transmit signals bidirectionally between the extracellular matrix and cytoplasmic domains.[9] [10]
Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainly focal adhesions .[8] [11] Integrin beta-1 mutants lose the ability to target to sites of focal 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 26 amino acids of the cytoplasmic domain in exon 6 are retained and then succeeded by a 12 amino acid stretch from an adjacent intronic region.[14] The integrin beta-1B isoform appears to act as a dominant negative in that it inhibits cell adhesion.[15] A second integrin beta-1 isoform , termed beta-1C, was described to have an additional 48 amino acids appended to the 26 amino acids in the cytoplasmic domain;[16] the function of this isoform was an inhibitory one on DNA synthesis in the G1 phase of the cell cycle .[17] The third isoform , termed beta-1D, is a striated muscle -specific isoform, which replaces the canonical beta-1A isoform in cardiac and skeletal muscle cells. This isoform is produced from splicing into a novel additional exon between exons 6 and 7. The cytoplasmic domain of integrin beta-1D replaces the distal 21 amino acids (present in integrin beta-1A) with an alternative stretch of 24 amino acids (13 unique).[18] [19]
Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,[19] appearing immediately following the fusion of myoblasts in C2C12 cell with rising levels throughout myofibrillar differentiation.[20] Integrin beta-1D is specifically localized to costameres and intercalated discs of cardiac muscle and costameres , myotendinous junctions and neuromuscular junctions of skeletal muscle , and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface of CHO cells resulted in tyrosine phosphorylation of pp125FAK and induced mitogen-activated protein kinase activation.[20]
Clinical significance
[ edit ]
In patients with limb girdle muscular dystrophy , type 2C, beta-1D integrin has been shown to be severely reduced in skeletal muscle biopsies, coordinate with a reduction in alpha 7B-integrin and filamin 2 .[21]
In patients with sensitive-motor polyneuropathy , levels of integrin alpha-7B , integrin beta-1D and agrin were significantly reduced nearly to undetectable levels; and this corresponded with lower mRNA levels.[22]
Interactions
[ edit ]
CD29 has been shown to interact with
CD46 ,[25]
CD9 ,[26] [27]
FHL2 ,[28]
Filamin ,[29] [30]
FLNB ,[29]
CD81 ,[27] [31]
GNB2L1 ,[32] [33]
ITGB1BP1 ,[34] [35]
LGALS8 ,[36]
MAP4K4 ,[37]
NME1 ,[38]
PKC alpha ,[32] [39]
TLN1 ,[40] [41]
TSPAN4 ,[42] and
YWHAB .[43]
References
[ edit ]
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025809 – Ensembl , May 2017
^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ 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 .
^ "Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)" .
^ a b c Hynes 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 .
^ a b Sastry 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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. doi :10.1006/bbrc.1995.2285 . PMID 7545396 .
^ a b van 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. doi :10.1016/0014-5793(95 )00814-p . PMID 7544298 . S2CID 86638879 .
^ a b Belkin 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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. doi :10.1006/bbrc.1996.0690 . PMID 8630057 .
^ a b Mazzocca 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 .
^ 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 .
^ a b van 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 .
^ 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 .
^ 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 .
^ a b Lee 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ Poinat P, De Arcangelis A, Sookhareea S, Zhu X, Hedgecock EM, Labouesse M, Georges-Labouesse E (Apr 2002). "A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans" . Current Biology . 12 (8 ): 622–31. Bibcode :2002CBio...12..622P . doi :10.1016/S0960-9822(02 )00764-9 . PMID 11967148 . S2CID 9977605 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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
[ edit ]
Armulik A (Jan 2002). "Splice variants of human beta 1 integrins: origin, biosynthesis and functions" . Frontiers in Bioscience . 7 (1–3): d219-27. doi :10.2741/armulik . PMID 11779688 .
Brakebusch C, Fässler R (Sep 2005). "beta 1 integrin function in vivo: adhesion, migration and more". Cancer and Metastasis Reviews . 24 (3 ): 403–11. doi :10.1007/s10555-005-5132-5 . PMID 16258728 . S2CID 24210890 .
External links
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t
e
1–50
51–100
101–150
151–200
201–250
251–300
301–350
t
e
Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:
see also cell surface receptor deficiencies
R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Integrin_beta_1&oldid=1216947931 "
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