A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment

A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment

The recruitment of substrates by the ser/thr protein phosphatase 2A (PP2A) is poorly understood, limiting our understanding of PP2A-regulated signaling. Recently, the first PP2A:B56 consensus binding motif, LxxIxE, was identified. However, most validated LxxIxE motifs bind PP2A:B56 with micromolar a...

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Bibliographic Details
Main Authors: Xinru Wang, Dimitriya H Garvanska, Isha Nasa, Yumi Ueki, Gang Zhang, Arminja N Kettenbach, Wolfgang Peti, Jakob Nilsson, Rebecca Page
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2020-03-01
Series:eLife
Subjects:
protein phosphatase
PP2A-B56
intrinsically disordered protein
dynamic, charge-charge interactions
KIF4A
structural and cell biology
Online Access:https://elifesciences.org/articles/55966

Internet

https://elifesciences.org/articles/55966

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