Jolinda A. Traugh

p21-activated protein kinase gamma-PAK in pituitary secretory granules phosphorylates prolactin.

Localization of p21-activated protein kinase gamma-PAK/Pak2 in the endoplasmic reticulum is required for induction of cytostasis.

Activation of Syk protein tyrosine kinase in response to osmotic stress requires interaction with p21-activated protein kinase Pak2/gamma-PAK.

Negative control of the Myc protein by the stress-responsive kinase Pak2.

Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk.

Regulation of the interaction of Pak2 with Cdc42 via autophosphorylation of serine 141.

Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2.

Phosphorylation of c-Abl by protein kinase Pak2 regulates differential binding of ABI2 and CRK.

Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange.

Reciprocally coupled residues crucial for protein kinase Pak2 activity calculated by statistical coupling analysis.