Gene interactions and pathways from curated databases and text-mining

◀ Back to PTK2

PTK2 — PXN

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Heidkamp et al., Circ Res 2002 : Furthermore, GFP-FRNK resulted in the loss of detectable FAK and paxillin in focal adhesions, which was accompanied by reduced levels of total paxillin and, ultimately, cell detachment and apoptosis
Hehlgans et al., Int J Radiat Biol 2007 : On the basis of the presented data, a precise correlation of adhesion-, serum- and PI3K mediated changes in PI3K/AKT and FAK/Paxillin/p130Cas signaling cascades was not found
Saito et al., Biol Pharm Bull 2008 (Wounds and Injuries) : TNIIIA2-treatment unaffected autophosphorylation of focal adhesion kinase ( FAK ), but induced its physical association with phospho-paxillin ( Tyr118 ), suggesting the FAK/paxillin dependent negative regulation of Rac activation
Aponte et al., Cancer Res 2008 (Disease Progression...) : Activation of platelet activating factor receptor and pleiotropic effects on tyrosine phospho-EGFR/Src/FAK/paxillin in ovarian cancer
Tang et al., Experimental biology and medicine (Maywood, N.J.) 2009 (Carcinoma, Hepatocellular...) : We suggest that by interaction with alpha 3beta 1 integrin, beta ig-h3 activates FAK-paxillin signaling linkage, leads to cytoskeleton reorganization, and thus enhances the metastatic potentials of human hepatoma cells
Koshman et al., Arterioscler Thromb Vasc Biol 2010 : L341S-FRNK affected FA binding kinetics ( assessed by total internal reflection fluorescnece [ TIRF ] microscopy and fluorescence recovery after photobleaching [ FRAP ] ) and reduced its steady-state paxillin interaction ( determined by coimmunoprecipitation )
Park et al., Biochim Biophys Acta 2013 : In conclusion, C ( 16 ) -Cer enhances mouse ESC migration through the regulation of PKC and FAK/Paxillin dependent N-WASP/Cdc42/Arp2/3 complex formation as well as through promoting the interaction between cofilin-1 or a-actinin-1/-4 and F-actin ... In conclusion, C ( 16 ) -Cer enhances mouse ESC migration through the regulation of PKC and FAK/Paxillin dependent N-WASP/Cdc42/Arp2/3 complex formation as well as through promoting the interaction between cofilin-1 or a-actinin-1/-4 and F-actin ... In conclusion, C ( 16 ) -Cer enhances mouse ESC migration through the regulation of PKC and FAK/Paxillin dependent N-WASP/Cdc42/Arp2/3 complex formation as well as through promoting the interaction between cofilin-1 or a-actinin-1/-4 and F-actin
Schaller et al., Mol Cell Biol 1995 : pp125FAK dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk ... We describe here conditions under which the phosphorylation of paxillin on tyrosine is pp125FAK dependent, supporting the hypothesis that paxillin phosphorylation is regulated by pp125FAK ... These observations suggest that paxillin serves as an adapter protein, similar to insulin receptor substrate 1, and that pp125FAK may regulate the formation of signaling complexes by directing the phosphorylation of paxillin on tyrosine
Schaller et al., J Cell Biol 1995 : Paxillin binding is independent of pp125FAK binding despite the fact that both bind to the same region of beta 1
Naruse et al., Oncogene 1998 : Moreover, suppression of pp125FAK expression by the antisense phosphorothioate oligodeoxynucleotides ( S-ODN ) in HUVECs resulted in inhibition of tyrosine phosphorylation of paxillin and the stretch dependent morphological changes