Leukemia

Tyr phosphorylation modulates binding preference in leukemia cells

Published in Cancer Weekly, March 21st, 2006

According to recent research from Germany, Tyr phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of P27(Kip1) in the acute promyelocytic leukemia cell line NB4.

"We have investigated the role of Tyr phosphorylation of the cyclin-dependent kinase (cdk) inhibitor p27(Kip1) using the acute promyelocytic leukemia cell line NB4 together with granulocyte colony-stimulating factor (G-CSF)," wrote C. Kardinal and colleagues, Hannover Medical School.

They wrote, "Short-term G-CSF stimulation resulted in a rapid Tyr dephosphorylation of p27(Kip1) accompanied by a change in its binding preferences to cdks. On...

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Source: Cancer Weekly (2006-03-21)

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