Cargando…
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...
Autores principales: | Wang, Xinru, Garvanska, Dimitriya H, Nasa, Isha, Ueki, Yumi, Zhang, Gang, Kettenbach, Arminja N, Peti, Wolfgang, Nilsson, Jakob, Page, Rebecca |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108865/ https://www.ncbi.nlm.nih.gov/pubmed/32195664 http://dx.doi.org/10.7554/eLife.55966 |
Ejemplares similares
-
Coupling of Cdc20 inhibition and activation by BubR1
por: Hein, Jamin B., et al.
Publicado: (2021) -
PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107
por: Fowle, Holly, et al.
Publicado: (2021) -
A highly conserved pocket on PP2A‐B56 is required for hSgo1 binding and cohesion protection during mitosis
por: Ueki, Yumi, et al.
Publicado: (2021) -
Mechanisms of site‐specific dephosphorylation and kinase opposition imposed by PP2A regulatory subunits
por: Kruse, Thomas, et al.
Publicado: (2020) -
Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis
por: Nasa, Isha, et al.
Publicado: (2018)