Integrin beta 1

Last updated
ITGB1
Protein ITGB1 PDB 1K11.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ITGB1 , CD29, FNRB, GPIIA, MDF2, MSK12, VLA-BETA, VLAB, integrin subunit beta 1
External IDs OMIM: 135630 MGI: 96610 HomoloGene: 22999 GeneCards: ITGB1
Orthologs
SpeciesHumanMouse
Entrez

3688

16412

Ensembl

ENSG00000150093

ENSMUSG00000025809

UniProt

P05556

P09055

RefSeq (mRNA)

NM_010578

RefSeq (protein)

NP_002202
NP_391988
NP_596867

NP_034708

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

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

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

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

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

CD29 has been shown to interact with

Related Research Articles

<span class="mw-page-title-main">Integrin</span> Instance of a defined set in Homo sapiens with Reactome ID (R-HSA-374573)

Integrins are transmembrane receptors that help cell-cell and cell-extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allows rapid and flexible responses to events at the cell surface.

<span class="mw-page-title-main">Laminin</span> Protein in the extracellular matrix

Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina. Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.

<span class="mw-page-title-main">Vinculin</span> Mammalian protein found in Homo sapiens

In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane.

<span class="mw-page-title-main">Paxillin</span> Protein-coding gene in the species Homo sapiens

Paxillin is a protein that in humans is encoded by the PXN gene. Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix. Mutations in PXN as well as abnormal expression of paxillin protein has been implicated in the progression of various cancers.

<span class="mw-page-title-main">Integrin-linked kinase</span> Protein-coding gene in the species Homo sapiens

Integrin-linked kinase is an enzyme that in humans is encoded by the ILK gene involved with integrin-mediated signal transduction. Mutations in ILK are associated with cardiomyopathies. It is a 59kDa protein originally identified in a yeast-two hybrid screen with integrin β1 as the bait protein. Since its discovery, ILK has been associated with multiple cellular functions including cell migration, proliferation, and adhesion.

<span class="mw-page-title-main">Integrin alpha 3</span> Mammalian protein found in Homo sapiens

Integrin alpha-3 is a protein that in humans is encoded by the ITGA3 gene. ITGA3 is an integrin alpha subunit. Together with beta-1 subunit, it makes up half of the α3β1 integrin duplex that plays a role in neural migration and corticogenesis, acted upon by such factors as netrin-1 and reelin.

<span class="mw-page-title-main">Integrin beta 3</span> Mammalian protein found in Homo sapiens

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene. CD61 is a cluster of differentiation found on thrombocytes.

Dystrobrevin is a protein that binds to dystrophin in the costamere of skeletal muscle cells. In humans, there are at least two isoforms of dystrobrevin, dystrobrevin alpha and dystrobrevin beta.

<span class="mw-page-title-main">PTK2</span> Protein-coding gene in humans

PTK2 protein tyrosine kinase 2 (PTK2), also known as focal adhesion kinase (FAK), is a protein that, in humans, is encoded by the PTK2 gene. PTK2 is a focal adhesion-associated protein kinase involved in cellular adhesion and spreading processes. It has been shown that when FAK was blocked, breast cancer cells became less metastatic due to decreased mobility.

<span class="mw-page-title-main">Integrin beta 4</span> Protein-coding gene in the species Homo sapiens

Integrin, beta 4 (ITGB4) also known as CD104, is a human gene.

<span class="mw-page-title-main">Alpha-actinin-2</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-2 is a protein which in humans is encoded by the ACTN2 gene. This gene encodes an alpha-actinin isoform that is expressed in both skeletal and cardiac muscles and functions to anchor myofibrillar actin thin filaments and titin to Z-discs.

<span class="mw-page-title-main">Integrin beta 5</span> Protein-coding gene in the species Homo sapiens

Integrin beta-5 is a protein that in humans is encoded by the ITGB5 gene.

<span class="mw-page-title-main">Integrin beta 6</span> Protein-coding gene in the species Homo sapiens

Integrin beta-6 is a protein that in humans is encoded by the ITGB6 gene. It is the β6 subunit of the integrin αvβ6. Integrins are αβ heterodimeric glycoproteins which span the cell’s membrane, integrating the outside and inside of the cell. Integrins bind to specific extracellular proteins in the extracellular matrix or on other cells and subsequently transduce signals intracellularly to affect cell behaviour. One α and one β subunit associate non-covalently to form 24 unique integrins found in mammals. While some β integrin subunits partner with multiple α subunits, β6 associates exclusively with the αv subunit. Thus, the function of ITGB6 is entirely associated with the integrin αvβ6.

<span class="mw-page-title-main">Integrin beta 7</span>

Integrin beta-7 is an integrin protein that in humans is encoded by the ITGB7 gene. It can pair with ITGA4 (CD49d) to form the heterodimeric integrin receptor α4β7, or with ITGAE (CD103) to form αEβ7.

<span class="mw-page-title-main">Integrin alpha 7</span>

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene. Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

<span class="mw-page-title-main">ITGB1BP1</span> Protein-coding gene in the species Homo sapiens

Integrin beta-1-binding protein 1 is a protein that in humans is encoded by the ITGB1BP1 gene.

<span class="mw-page-title-main">Integrin alpha 9</span> Protein-coding gene in the species Homo sapiens

Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene. Cytogenetic location: 3p22.2

<span class="mw-page-title-main">TLN1</span> Protein-coding gene in the species Homo sapiens

Talin-1 is a protein that in humans is encoded by the TLN1 gene. Talin-1 is ubiquitously expressed, and is localized to costamere structures in cardiac and skeletal muscle cells, and to focal adhesions in smooth muscle and non-muscle cells. Talin-1 functions to mediate cell-cell adhesion via the linkage of integrins to the actin cytoskeleton and in the activation of integrins. Altered expression of talin-1 has been observed in patients with heart failure, however no mutations in TLN1 have been linked with specific diseases.

<span class="mw-page-title-main">TLN2</span> Protein-coding gene in the species Homo sapiens

Talin-2 is a protein in humans that is encoded by the TLN2 gene. It belongs to the talin protein family. This gene encodes a protein related to talin-1, a cytoskeletal protein that plays a significant role in the assembly of actin filaments. Talin-2 is expressed at high levels in cardiac muscle and functions to provide linkages between the extracellular matrix and actin cytoskeleton at costamere structures to transduce force laterally.

Integrin α4β7 is an integrin heterodimer composed of CD49d (alpha-4) subunit and beta-7 subunit noncovalently linked. LPAM-1 is expressed on the cell surface of leukocytes. This receptor is involved in lymphocyte trafficking pathway to site of inflammation in intestinal tissues.

References

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  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025809 - Ensembl, May 2017
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  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. doi:10.1006/bbrc.1996.0690. PMID   8630057.
  27. 1 2 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.
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  29. 1 2 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.
  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. 1 2 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.
  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.
  37. ↑ 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.
  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.

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