Mass spectrometry studies of Wip1 phosphatase complex formation and post-translational modification

Wednesday, September 24, 2014 — Poster Session IV
10:00 a.m. –12:00 p.m.	FAES Academic Center	NCI	CANCER-12

Authors

• L.M. Jenkins
• S.J. Mazur
• E. Appella

Abstract

Wip1, the product of the PPM1D gene, is a stress-response serine/threonine protein phosphatase that regulates multiple biological processes. Following DNA damage-inducing stress, Wip1 dephosphorylates several proteins including p53, ATM, γ-H2AX, and p38 MAPK, thereby repressing DNA repair, cell cycle arrest, and apoptosis. In addition, Wip1 has been shown to regulate ageing through Wnt signaling. Wip1 is amplified or overexpressed in a number of human cancers, and this status is associated with a poorer prognosis. Mice lacking Wip1 expression have been found to be resistant to tumorigenesis. In order to better understand the regulation and roles of Wip1, we have used mass spectrometry techniques to map sites of Wip1 post-translational modification and identify interacting proteins. These studies open new avenues of investigation regarding Wip1 function and means to inhibit its activities in tumors.

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