MassIVE MSV000084245

Complete Public PXD015205

Determinants of site-specific dephosphorylation by PP2A-B56

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Description

The tumor suppressor PP2A is a major cellular protein phosphatase that regulates numerous cellular processes through the formation of holoenzymes containing distinct regulatory B-subunits. However, the determinants of differential substrate dephosphorylation by PP2A are poorly understood. Here, we develop a specific genetically encoded inhibitor of PP2A-B56 and perform global phosphoproteomic studies to identify hundreds of regulated phosphorylation sites. We show that PP2A-B56 substrate specificity is controlled by affinity and position of B56 binding motifs and that PP2A active site preference is determined by the B-subunit. These insights uncover PP2A-B56 as a novel negative regulator of ADAM17 mediated growth factor signalling and tumor development. Collectively our work identifies basic principles of PP2A-B56 specificity with broad implications for understanding signalling in eukaryotes. [doi:10.25345/C57H30] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: PP2A ; B56 ; phosphatase ; holoenzyme ; dephosphorylation ; motif ; ADAM17 ; growth factor ; tumor

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Principal Investigators:
(in alphabetical order) 		Arminja Kettenbach, The Geisel School of Medicine at Dartmouth, United States
Submitting User: madamo
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