Integrin beta 1

Source: Wikipedia, the free encyclopedia.
ITGB1
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl
UniProt
RefSeq (mRNA)

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 as CD29, is a

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

.

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

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,

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

In patients with sensitive-motor

mRNA levels.[22]

Interactions

CD29 has been shown to

interact
with

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000150093Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025809Ensembl, 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. S2CID 36485270
    .
  6. ^ "Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)".
  7. ^
    S2CID 32774108
    .
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Further reading

External links