Identification of novel LIMK2 phosphorylation substrates

Breast cancer is the most common and a lethal form of cancer diagnosed in women worldwide. Although, effective treatment options for primary tumors are available, the majority of breast cancer-related deaths is caused by invasion of cells from primary tumor results in metastatic progression. Here we used a phopshoproteomic analysis to identify new targets of pro-invasive LIM kinase 2 (LIMK2) in invasive breast cancer cell lines. We show that Serine Arginine protein kinase 1 (SRPK1) is phosphorylated and activated by LIMK2 and LIMK2-SRPK1 signaling axis mediate the invasive behavior of breast cancer cells.