Complex structures of Rsu1 and PINCH1 reveal a regulatory mechanism of the ILK/PINCH/Parvin complex for F-actin dynamics. | Complex structures of Rsu1 and PINCH1 reveal a regulatory mechanism of the ILK/PINCH/Parvin complex for F-actin dynamics. Yang H, Lin L, Sun K, Zhang T, Chen W, Li L, Xie Y, Wu C, Wei Z, Yu C., Free PMC Article | 02/5/2022 |
A novel signaling pathway consisting of alpha-parvin, G3BP2, and TWIST1 regulates breast cancer progression and metastasis, this suggests that the activation of this signaling pathway is a key factor for driving the progression and poor clinical outcome of human ER-negative breast cancer. | α-Parvin promotes breast cancer progression and metastasis through interaction with G3BP2 and regulation of TWIST1 signaling. Sun Y, Ding Y, Guo C, Liu C, Ma P, Ma S, Wang Z, Liu J, Qian T, Ma L, Deng Y, Wu C. | 12/14/2019 |
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 | A-to-I miR-378a-3p editing can prevent melanoma progression via regulation of PARVA expression. Velazquez-Torres G, Shoshan E, Ivan C, Huang L, Fuentes-Mattei E, Paret H, Kim SJ, Rodriguez-Aguayo C, Xie V, Brooks D, Jones SJM, Robertson AG, Calin G, Lopez-Berenstein G, Sood A, Bar-Eli M., Free PMC Article | 09/22/2018 |
Protein expression of alpha-Parvin increases with colorectal cancer progression. | Focal Adhesion Proteins α- and β-Parvin are Overexpressed in Human Colorectal Cancer and Correlate with Tumor Progression. Bravou V, Antonacopoulou A, Papanikolaou S, Nikou S, Lilis I, Giannopoulou E, Kalofonos HP. | 04/30/2016 |
PARVA promotes metastasis by modulating ILK signalling pathway in lung adenocarcinoma | PARVA promotes metastasis by modulating ILK signalling pathway in lung adenocarcinoma. Huang AH, Pan SH, Chang WH, Hong QS, Chen JJ, Yu SL., Free PMC Article | 01/23/2016 |
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. | Endothelial alpha-parvin controls integrity of developing vasculature and is required for maintenance of cell-cell junctions. Fraccaroli A, Pitter B, Taha AA, Seebach J, Huveneers S, Kirsch J, Casaroli-Marano RP, Zahler S, Pohl U, Gerhardt H, Schnittler HJ, Montanez E., Free PMC Article | 08/29/2015 |
alpha-Parvin, a pseudopodial constituent, was found to promote migration of breast cancer cells and to be expressed exclusively by Invasive lobular carcinoma | α-Parvin, a pseudopodial constituent, promotes cell motility and is associated with lymph node metastasis of lobular breast carcinoma. Ito M, Hagiyama M, Mimae T, Inoue T, Kato T, Yoneshige A, Nakanishi J, Kondo T, Okada M, Ito A. | 10/4/2014 |
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. | Suppression of actopaxin impairs hepatocellular carcinoma metastasis through modulation of cell migration and invasion. Ng L, Tung-Ping Poon R, Yau S, Chow A, Lam C, Li HS, Chung-Cheung Yau T, Law WL, Pang R. | 01/18/2014 |
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 | Beta2-adaptin binds actopaxin and regulates cell spreading, migration and matrix degradation. Pignatelli J, Jones MC, LaLonde DP, Turner CE., Free PMC Article | 06/15/2013 |
alpha-parvin, beta-parvin and migfilin were expressed in tumor cells in 53%, 2%, 28% and 53% of effusions and 57%, 20%, 83% and 25% of solid lesions, respectively. | Migfilin, α-parvin and β-parvin are differentially expressed in ovarian serous carcinoma effusions, primary tumors and solid metastases. Davidson B, Holth A, Nguyen MT, Tropé CG, Wu C., Free PMC Article | 03/30/2013 |
Actopaxin phosphorylation is required for matrix degradation and cell invasion via regulation of Rho GTPase signaling. | Actopaxin (α-parvin) phosphorylation is required for matrix degradation and cancer cell invasion. Pignatelli J, LaLonde SE, LaLonde DP, Clarke D, Turner CE., Free PMC Article | 01/12/2013 |
results also identify the integrin-linked kinase (ILK) and alpha-parvin proteins as a new molecular partner and target, respectively, of the Lnk adaptor. | LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets α-parvin to control cell adhesion and migration. Devallière J, Chatelais M, Fitau J, Gérard N, Hulin P, Velazquez L, Turner CE, Charreau B., Free PMC Article | 08/25/2012 |
the alpha-parvin CH2-paxillin LD1 complex has a role in focal adhesion assembly | The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly. Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J., Free PMC Article | 12/27/2010 |
Meta-analysis and genome-wide association study of gene-disease association. (HuGE Navigator) | Genomic variation associated with mortality among adults of European and African ancestry with heart failure: the cohorts for heart and aging research in genomic epidemiology consortium. Morrison AC, Felix JF, Cupples LA, Glazer NL, Loehr LR, Dehghan A, Demissie S, Bis JC, Rosamond WD, Aulchenko YS, Wang YA, Haritunians T, Folsom AR, Rivadeneira F, Benjamin EJ, Lumley T, Couper D, Stricker BH, O'Donnell CJ, Rice KM, Chang PP, Hofman A, Levy D, Rotter JI, Fox ER, Uitterlinden AG, Wang TJ, Psaty BM, Willerson JT, van Duijn CM, Boerwinkle E, Witteman JC, Vasan RS, Smith NL., Free PMC Article | 06/30/2010 |
An unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell. | Structural analysis of the interactions between paxillin LD motifs and alpha-parvin. Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble ME, Hoellerer MK., Free PMC Article | 01/21/2010 |
Phosphorylation of actopaxin regulates cell spreading and migration. | Phosphorylation of actopaxin regulates cell spreading and migration. Clarke DM, Brown MC, LaLonde DP, Turner CE., Free PMC Article | 01/21/2010 |
the association between actopaxin and TESK1, which is likely regulated by phosphorylation of actopaxin, regulates TESK1 activity and subsequent cellular spreading on fibronectin | Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin. LaLonde DP, Brown MC, Bouverat BP, Turner CE. | 01/21/2010 |
Mammalian parvins are likely to have arisen late in evolution from gene duplication as they share a remarkably similar exon/intron organization. | Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans. Korenbaum E, Olski TM, Noegel AA. | 01/21/2010 |
inhibition of the ILK-alpha-parvin complex is sufficient, although not necessary, for promotion of apoptosis | Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. Zhang Y, Chen K, Tu Y, Wu C. | 01/21/2010 |