◀ Back to PXN

IGF1 — PXN

Pathways - manually collected, often from reviews:

• NCI Pathway Database IGF1 pathway: IGF-1R heterotetramer/IGF1/IRS1 complex (IGF1R-IGF1-IRS1) → Paxillin (PXN) (modification, activates) Butler et al., J Biol Chem 1997, Fagerström et al., J Biol Chem 1998, Casamassima et al., J Biol Chem 1998
  Evidence: assay, physical interaction
• NCI Pathway Database IGF1 pathway: IGF-1R heterotetramer/IGF1/IRS1 complex (IGF1R-IGF1-IRS1) → Crk/p130 Cas/Paxillin complex (CRK-BCAR1-PXN) (modification, activates)
  Butler et al., J Biol Chem 1997, Fagerström et al., J Biol Chem 1998, Casamassima et al., J Biol Chem 1998
  Evidence: assay, physical interaction

Text-mined interactions from Literome

Mañes et al., Mol Cell Biol 1999 (Neoplasm Invasiveness) : On the other hand, IGF-I promotes the association of insulin receptor substrate 1 with the focal adhesion kinase ( FAK ), paxillin , and the tyrosine phosphatase SHP-2, resulting in FAK and paxillin dephosphorylation ... On the other hand, IGF-I promotes the association of insulin receptor substrate 1 with the focal adhesion kinase ( FAK ), paxillin , and the tyrosine phosphatase SHP-2, resulting in FAK and paxillin dephosphorylation
Tai et al., Cancer Res 2003 (Multiple Myeloma) : In addition, IGF-I triggers polymerization of F-actin, induces phosphorylation of p125(FAK) and paxillin , and enhances beta1 integrin interaction with these focal adhesion proteins ... In addition, IGF-I triggers polymerization of F-actin, induces phosphorylation of p125(FAK) and paxillin , and enhances beta1 integrin interaction with these focal adhesion proteins
Furundzija et al., Biochem Biophys Res Commun 2010 (Atherosclerosis) : Pharmacological blocking experiments with specific inhibitors of Akt, PKC and p38 MAP-kinase revealed that IGF-1 dependent activation of focal adhesion kinase ( FAK ) and paxillin , and consecutively IGF-1 facilitated migration, required IGF-1/IGF-1R mediated PI3-kinase/PKC/p38 dependent integrin inside-out signaling ... Pharmacological blocking experiments with specific inhibitors of Akt, PKC and p38 MAP-kinase revealed that IGF-1 dependent activation of focal adhesion kinase ( FAK ) and paxillin , and consecutively IGF-1 facilitated migration, required IGF-1/IGF-1R mediated PI3-kinase/PKC/p38 dependent integrin inside-out signaling
Genua et al., PloS one 2012 (Carcinoma...) : These effects require IGF-I induced Akt- and MAPK dependent activation of paxillin ... FAK and its homolog Proline-rich tyrosine kinase 2 (Pyk2) modulate paxillin activation ; however, their role in regulating IGF-IR dependent signaling and motility in bladder cancer has not been established
Casamassima et al., J Biol Chem 1998 : Insulin-like growth factor I stimulates tyrosine phosphorylation of p130 ( Cas ), focal adhesion kinase, and paxillin ... IGF-I induced p130 ( Cas ), p125(Fak), and paxillin tyrosine phosphorylation could be dissociated from mitogen activated protein kinase kinase, p70 ( S6K ), and protein kinase C activation ... In contrast, the structurally unrelated phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 markedly attenuated the increase in tyrosine phosphorylation of p130 ( Cas ), p125(Fak), and paxillin induced by IGF-I ... Thus, our results identified a phosphatidylinositol 3-kinase dependent pathway that requires the integrity of the actin cytoskeleton to induce tyrosine phosphorylation of p130 ( Cas ), p125(Fak), and paxillin in response to IGF-I and suggest that tyrosine phosphorylation of these focal adhesion proteins, together with the recruitment of c-Crk into a complex with p130 ( Cas ), may play a novel role in IGF-I signal transduction