Abstract
| Bidragets oversatte titel | Et bindings motiv for PP4 fosfatasen: NA |
|---|---|
| Originalsprog | Engelsk |
| Tidsskrift | Molecular Cell |
| Vol/bind | 76 |
| Udgave nummer | 6 |
| Sider (fra-til) | 953-964.e6 |
| ISSN | 1097-2765 |
| DOI | |
| Status | Udgivet - 2019 |
Bibliografisk note
Copyright © 2019 Elsevier Inc. All rights reserved.Adgang til dokumentet
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A Consensus Binding Motif for the PP4 Protein Phosphatase. / Ueki, Yumi; Kruse, Thomas; Weisser, Melanie Bianca; Sundell, Gustav N; Larsen, Marie Sofie Yoo; Mendez, Blanca Lopez; Jenkins, Nicole P; Garvanska, Dimitriya H; Cressey, Lauren; Zhang, Gang; Davey, Norman; Montoya, Guillermo; Ivarsson, Ylva; Kettenbach, Arminja N; Nilsson, Jakob.
I: Molecular Cell, Bind 76, Nr. 6, 2019, s. 953-964.e6.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - A Consensus Binding Motif for the PP4 Protein Phosphatase
AU - Ueki, Yumi
AU - Kruse, Thomas
AU - Weisser, Melanie Bianca
AU - Sundell, Gustav N
AU - Larsen, Marie Sofie Yoo
AU - Mendez, Blanca Lopez
AU - Jenkins, Nicole P
AU - Garvanska, Dimitriya H
AU - Cressey, Lauren
AU - Zhang, Gang
AU - Davey, Norman
AU - Montoya, Guillermo
AU - Ivarsson, Ylva
AU - Kettenbach, Arminja N
AU - Nilsson, Jakob
N1 - Copyright © 2019 Elsevier Inc. All rights reserved.
PY - 2019
Y1 - 2019
N2 - Dynamic protein phosphorylation constitutes a fundamental regulatory mechanism in all organisms. Phosphoprotein phosphatase 4 (PP4) is a conserved and essential nuclear serine and threonine phosphatase. Despite the importance of PP4, general principles of substrate selection are unknown, hampering the study of signal regulation by this phosphatase. Here, we identify and thoroughly characterize a general PP4 consensus-binding motif, the FxxP motif. X-ray crystallography studies reveal that FxxP motifs bind to a conserved pocket in the PP4 regulatory subunit PPP4R3. Systems-wide in silico searches integrated with proteomic analysis of PP4 interacting proteins allow us to identify numerous FxxP motifs in proteins controlling a range of fundamental cellular processes. We identify an FxxP motif in the cohesin release factor WAPL and show that this regulates WAPL phosphorylation status and is required for efficient cohesin release. Collectively our work uncovers basic principles of PP4 specificity with broad implications for understanding phosphorylation-mediated signaling in cells.
AB - Dynamic protein phosphorylation constitutes a fundamental regulatory mechanism in all organisms. Phosphoprotein phosphatase 4 (PP4) is a conserved and essential nuclear serine and threonine phosphatase. Despite the importance of PP4, general principles of substrate selection are unknown, hampering the study of signal regulation by this phosphatase. Here, we identify and thoroughly characterize a general PP4 consensus-binding motif, the FxxP motif. X-ray crystallography studies reveal that FxxP motifs bind to a conserved pocket in the PP4 regulatory subunit PPP4R3. Systems-wide in silico searches integrated with proteomic analysis of PP4 interacting proteins allow us to identify numerous FxxP motifs in proteins controlling a range of fundamental cellular processes. We identify an FxxP motif in the cohesin release factor WAPL and show that this regulates WAPL phosphorylation status and is required for efficient cohesin release. Collectively our work uncovers basic principles of PP4 specificity with broad implications for understanding phosphorylation-mediated signaling in cells.
U2 - 10.1016/j.molcel.2019.08.029
DO - 10.1016/j.molcel.2019.08.029
M3 - Journal article
C2 - 31585692
VL - 76
SP - 953-964.e6
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 6
ER -