In a recent study:
Wu-Zhang, Schramm, Nabavi, Malinow, Newton (2012). Cellular Pharmacology of Protein Kinase Mzeta (PKMzeta) Contrasts with its In Vitro Profile. The Journal of Biological Chemistry.
At first I skimmed through and saw they used FRET and thought it would be easy one to argue against. Then I read it. ZIP doesn’t affect the phosphorylation rate of PKMzeta (on any substrate empirically shown to be phosphorylated by PKMz). They showed this effect using simple immunoblotting methods, not just FRET. I can’t believe this hasn’t been done already. Do you have any arguments against the findings?
SPECIAL THANKS FOR THE CONSTRUCTIVE COMMENTARY FROM
Dr. Alexandra Newton (the article author) who’s research focuses on the functional mechanisms of phospholipase and kinase (PLC & PI3K) signaling pathways; and Dr. Todd Sacktor, who’s a long-standing pioneer of research on protein kinase C (PKC) isozymes in learning and memory.
This publication may be considered a direct response by Yao and Sacktor to the Wu-Zhang paper mentioned above
Matching biochemical and functional efficacies confirm ZIP as a potent competitive inhibitor of PKMz in neurons by Yudong Yao, Charles Shao, Desingarao Jothianandan, Andrew Tcherepanov, Harel Shouval, Todd Charlton Sacktor*