Functional role of PRMT5 for the RASSF1A-mediated tumor suppressive functions

点击翻译按钮获取中文摘要

We have identified protein arginine methyltransferase 5 (PRMT5) as a novel interacting protein with RASSF1A by peptide mass fingerprinting. Also, we found that co-expression of RASSF1A and PRMT5 in COS-7 cells led to partial re-localization of PRMT5 from cytosol to circular microtubule ring where it became strongly co-localized with RASSF1A. Also we found that the RASSF1A associated serine/threonine kinases; Mst1/2 and LATS, which were involved in the Hippo tumor suppressor pathway, translocated from cytosol to microtubule network on co-expression with RASSF1A. The results obtained suggest that RASSF1A links PRMT5 to microtubules and PRMT5-RASSF1A interaction plays a role in microtubule organization and that RASSF1A may play a novel role in bridging PRMT5 to arginine-methylation on microtubule, where it may play a role in modulating the RASSF1A-mediated tumor suppressive functions.