The Dynamics of a novel protein complex involved in RNA processing and cell cycle regulation

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Wilms' tumor 1-associating protein (WTAP) has been reported to be a ubiquitously expressed nuclear protein and supposed to have a role in pre-mRNA splicing. We have reported that WTAP is involved in the stability of cyclin A2 mRNA thereby regulates the cell cycle and WTAP knockout mice exhibited proliferative failure with death at early embryonic stage. In this study, we have developed a method for the functional analysis of protein-protein interactions for the endogenous proteins, by affinity purification mass spectrometry using magnetic beads and high-affinity antibodies. Using the method, we identified several binding proteins of WTAP, including vrilizer homolog, E3 ubiquitin ligase, SR proteins and RNA bindin proteins. Furthermore we found the compositional changes of WTAP protein complex in cell cycle, indicating a relation to cell cle regulation of WTAP protein complex.