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Abstract
In certain cell types, patelet-derived growth factor (PDGF) suppresses epidermal growth factor (EGF)-induced activation of the c-Jun N-terminal kinase (JNK). The Protein Kinase C (PKC) family of serine-threonine kinases has been implicated in this process. Bagowski et al . now report that Protein Kinase D (PKD) is critical to this transmodulation event. PKD is a kinase related to PKC, and is activated by PKC in response to PDGF stimulation. PKD-mediated transmodulation of EGF signaling by PDGF required phosphorylation of two threonine residues in the juxtamembrane region of the EGF receptor. It is still not clear if PKD works alone or with other kinases to phosphorylate the EGF receptor. Bagowski, C.P., Stein-Gerlach, M., Choidas, A., and Ullrich, A. (1999) Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. EMBO J . 18 : 5567-5576. [Abstract] [Full Text]
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