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Abstract
STAT3, a member of the signal transducer and activator of transcription (STAT) family of transcription factors, is a known regulator of cell motility through its transcriptional activating functions. However, new evidence suggests a novel role for non–tyrosine-phosphorylated and cytoplasmically localized STAT3 in mediating cell migration by disrupting an interaction between microtubules and one of its partners, stathmin. The association of STAT3 with stathmin potentiates microtubule polymerization and cell movement.
