Figure 5.
Figure 5. Model for signaling of cytoskeletal F-actin polymerization. Gβγ released after GPCR ligation activates PI3K-dependent and PI3K-independent pathways of F-actin polymerization. The PI3K pathway may involve the class IA PI3Ks, which are primed (dashed arrow) with GM-CSF via p85 phosphorylation. The PI3K-pathway is also dependent on Akt/PKB and PKC-ζ.25 The PI3K-independent pathway is primed with insulin (dashed arrow) via an unknown mechanism, which does not require PI3K activation. The PI3K-independent pathway is dependent on Src tyrosine kinases, RhoA, Rho-associated kinase (ROCK), NADPH oxidase, and PKA.25 The inhibition of this pathway by PI3K-SH2-OMT shows that it is dependent on an unspecified SH2 domain protein (Figures S1-S3).

Model for signaling of cytoskeletal F-actin polymerization. Gβγ released after GPCR ligation activates PI3K-dependent and PI3K-independent pathways of F-actin polymerization. The PI3K pathway may involve the class IA PI3Ks, which are primed (dashed arrow) with GM-CSF via p85 phosphorylation. The PI3K-pathway is also dependent on Akt/PKB and PKC-ζ.25  The PI3K-independent pathway is primed with insulin (dashed arrow) via an unknown mechanism, which does not require PI3K activation. The PI3K-independent pathway is dependent on Src tyrosine kinases, RhoA, Rho-associated kinase (ROCK), NADPH oxidase, and PKA.25  The inhibition of this pathway by PI3K-SH2-OMT shows that it is dependent on an unspecified SH2 domain protein (Figures S1-S3).

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