[HTML][HTML] Phosphorylation by glycogen synthase kinase-3 controls c-myc proteolysis and subnuclear localization
MA Gregory, Y Qi, SR Hann - Journal of Biological Chemistry, 2003 - ASBMB
The c-Myc protein is a transcription factor that is a central regulator of cell growth and
proliferation. Thr-58 is a major phosphorylation site in c-Myc and is a mutational hotspot in
Burkitt's and other aggressive human lymphomas, indicating that Thr-58 phosphorylation
restricts the oncogenic potential of c-Myc. Mutation of Thr-58 is also associated with
increased c-Myc protein stability. Here we show that inhibition of glycogen synthase kinase-
3 (GSK-3) activity with lithium increases c-Myc stability and inhibits phosphorylation of c-Myc …
proliferation. Thr-58 is a major phosphorylation site in c-Myc and is a mutational hotspot in
Burkitt's and other aggressive human lymphomas, indicating that Thr-58 phosphorylation
restricts the oncogenic potential of c-Myc. Mutation of Thr-58 is also associated with
increased c-Myc protein stability. Here we show that inhibition of glycogen synthase kinase-
3 (GSK-3) activity with lithium increases c-Myc stability and inhibits phosphorylation of c-Myc …