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IGF1 — PXN
Pathways - manually collected, often from reviews:
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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
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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