A Consensus Binding Motif for the PP4 Protein Phosphatase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Molecular Cell, Vol. 76, No. 6, 2019, p. 953-964.e6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Ueki, Y, Kruse, T, Weisser, MB, Sundell, GN, Larsen, MSY, Mendez, BL, Jenkins, NP, Garvanska, DH, Cressey, L, Zhang, G, Davey, N, Montoya, G, Ivarsson, Y, Kettenbach, AN & Nilsson, J 2019, 'A Consensus Binding Motif for the PP4 Protein Phosphatase', Molecular Cell, vol. 76, no. 6, pp. 953-964.e6. https://doi.org/10.1016/j.molcel.2019.08.029

APA

Ueki, Y., Kruse, T., Weisser, M. B., Sundell, G. N., Larsen, M. S. Y., Mendez, B. L., Jenkins, N. P., Garvanska, D. H., Cressey, L., Zhang, G., Davey, N., Montoya, G., Ivarsson, Y., Kettenbach, A. N., & Nilsson, J. (2019). A Consensus Binding Motif for the PP4 Protein Phosphatase. Molecular Cell, 76(6), 953-964.e6. https://doi.org/10.1016/j.molcel.2019.08.029

Vancouver

Ueki Y, Kruse T, Weisser MB, Sundell GN, Larsen MSY, Mendez BL et al. A Consensus Binding Motif for the PP4 Protein Phosphatase. Molecular Cell. 2019;76(6):953-964.e6. https://doi.org/10.1016/j.molcel.2019.08.029

Author

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. / A Consensus Binding Motif for the PP4 Protein Phosphatase. In: Molecular Cell. 2019 ; Vol. 76, No. 6. pp. 953-964.e6.

Bibtex

@article{ff2b91a63f404b1c8682cfc3699b59e1,
title = "A Consensus Binding Motif for the PP4 Protein Phosphatase",
abstract = "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.",
author = "Yumi Ueki and Thomas Kruse and Weisser, {Melanie Bianca} and Sundell, {Gustav N} and Larsen, {Marie Sofie Yoo} and Mendez, {Blanca Lopez} and Jenkins, {Nicole P} and Garvanska, {Dimitriya H} and Lauren Cressey and Gang Zhang and Norman Davey and Guillermo Montoya and Ylva Ivarsson and Kettenbach, {Arminja N} and Jakob Nilsson",
note = "Copyright {\textcopyright} 2019 Elsevier Inc. All rights reserved.",
year = "2019",
doi = "10.1016/j.molcel.2019.08.029",
language = "English",
volume = "76",
pages = "953--964.e6",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "6",

}

RIS

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 -

ID: 228409097