Article Abstract

Novel insights into the oncogenic function of the SMYD3 lysine methyltransferase

Authors: Pawel K. Mazur, Or Gozani, Julien Sage, Nicolas Reynoird

Abstract

SMYD3 is a member of the SMYD family of lysine methyltransferases (KMTs). In humans, there are five SMYD members (SMYD1–5) that are characterized by the presence of a split catalytic SET domain interrupted by a MYND zinc finger domain. The MYND domain is thought to potentially mediate DNA or protein binding but a clear function is yet to be established. SMYD homologs have been described in a wide range of organisms, such as zebrafish, drosophila and budding yeast (1,2). While methylation activity has been clearly established for SMYD2 and SMYD3 (3-6), the activities of SMYD1, 4 and 5 are not well understood.