PARVA Antibody

1. edited form of miR-378a-3p preferentially binds to the 3'-UTR of the PARVA oncogene and inhibits its expression, thus preventing the progression of melanoma towards the malignant phenotype PMID: 29386624
2. Protein expression of alpha-Parvin increases with colorectal cancer progression. PMID: 26115385
3. PARVA promotes metastasis by modulating ILK signalling pathway in lung adenocarcinoma PMID: 25738875
4. alpha-pv-deficient HUVECs show reduced stable adherens junctions, decreased monolayer formation, and impaired motility, associated with reduced formation of integrin-mediated cell-extracellular matrix adhesion structures and an altered actin cytoskeleton. PMID: 25925587
5. alpha-Parvin, a pseudopodial constituent, was found to promote migration of breast cancer cells and to be expressed exclusively by Invasive lobular carcinoma PMID: 24496929
6. Actopaxin plays a role in hepatocellular carcinoma progression and metastasis, by way of regulation of cell invasiveness and motility, an epithelial-mesenchymal transition process, and chemosensitivity to cytotoxic drugs. PMID: 23504997
7. beta2-adaptin is shown to bind to the focal adhesion protein actopaxin and localize to focal adhesions during cells spreading in an actopaxin dependent manner PMID: 23056266
8. Actopaxin phosphorylation is required for matrix degradation and cell invasion via regulation of Rho GTPase signaling. PMID: 22955285
9. results also identify the integrin-linked kinase (ILK) and alpha-parvin proteins as a new molecular partner and target, respectively, of the Lnk adaptor. PMID: 22441983
10. the alpha-parvin CH2-paxillin LD1 complex has a role in focal adhesion assembly PMID: 18508764
11. Mammalian parvins are likely to have arisen late in evolution from gene duplication as they share a remarkably similar exon/intron organization. PMID: 11722847
12. inhibition of the ILK-alpha-parvin complex is sufficient, although not necessary, for promotion of apoptosis PMID: 15284246
13. Phosphorylation of actopaxin regulates cell spreading and migration. PMID: 15353548
14. the association between actopaxin and TESK1, which is likely regulated by phosphorylation of actopaxin, regulates TESK1 activity and subsequent cellular spreading on fibronectin PMID: 15817463
15. An unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell. PMID: 18940607

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HGNC: 14652

OMIM: 608120

KEGG: hsa:55742

STRING: 9606.ENSP00000334008

UniGene: Hs.432914