A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase

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

Standard

A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase. / Hertz, Emil Peter Thrane; Kruse, Thomas; Davey, Norman E; López-Méndez, Blanca; Sigurdsson, Jón Otti; Montoya, Guillermo; Olsen, Jesper V; Nilsson, Jakob.

In: Molecular Cell, Vol. 63, No. 4, 2016, p. 686-695.

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

Harvard

Hertz, EPT, Kruse, T, Davey, NE, López-Méndez, B, Sigurdsson, JO, Montoya, G, Olsen, JV & Nilsson, J 2016, 'A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase', Molecular Cell, vol. 63, no. 4, pp. 686-695. https://doi.org/10.1016/j.molcel.2016.06.024

APA

Hertz, E. P. T., Kruse, T., Davey, N. E., López-Méndez, B., Sigurdsson, J. O., Montoya, G., Olsen, J. V., & Nilsson, J. (2016). A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase. Molecular Cell, 63(4), 686-695. https://doi.org/10.1016/j.molcel.2016.06.024

Vancouver

Hertz EPT, Kruse T, Davey NE, López-Méndez B, Sigurdsson JO, Montoya G et al. A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase. Molecular Cell. 2016;63(4):686-695. https://doi.org/10.1016/j.molcel.2016.06.024

Author

Hertz, Emil Peter Thrane ; Kruse, Thomas ; Davey, Norman E ; López-Méndez, Blanca ; Sigurdsson, Jón Otti ; Montoya, Guillermo ; Olsen, Jesper V ; Nilsson, Jakob. / A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase. In: Molecular Cell. 2016 ; Vol. 63, No. 4. pp. 686-695.

Bibtex

@article{32846e55995a41e9899cf0944572f8bd,

title = "A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase",

abstract = "Dynamic protein phosphorylation is a fundamental mechanism regulating biological processes in all organisms. Protein phosphatase 2A (PP2A) is the main source of phosphatase activity in the cell, but the molecular details of substrate recognition are unknown. Here, we report that a conserved surface-exposed pocket on PP2A regulatory B56 subunits binds to a consensus sequence on interacting proteins, which we term the LxxIxE motif. The composition of the motif modulates the affinity for B56, which in turn determines the phosphorylation status of associated substrates. Phosphorylation of amino acid residues within the motif increases B56 binding, allowing integration of kinase and phosphatase activity. We identify conserved LxxIxE motifs in essential proteins throughout the eukaryotic domain of life and in human viruses, suggesting that the motifs are required for basic cellular function. Our study provides a molecular description of PP2A binding specificity with broad implications for understanding signaling in eukaryotes.",

author = "Hertz, {Emil Peter Thrane} and Thomas Kruse and Davey, {Norman E} and Blanca L{\'o}pez-M{\'e}ndez and Sigurdsson, {J{\'o}n Otti} and Guillermo Montoya and Olsen, {Jesper V} and Jakob Nilsson",

year = "2016",

doi = "10.1016/j.molcel.2016.06.024",

language = "English",

volume = "63",

pages = "686--695",

journal = "Molecular Cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "4",

}

RIS

TY - JOUR

T1 - A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase

AU - Hertz, Emil Peter Thrane

AU - Kruse, Thomas

AU - Davey, Norman E

AU - López-Méndez, Blanca

AU - Sigurdsson, Jón Otti

AU - Montoya, Guillermo

AU - Olsen, Jesper V

AU - Nilsson, Jakob

PY - 2016

Y1 - 2016

N2 - Dynamic protein phosphorylation is a fundamental mechanism regulating biological processes in all organisms. Protein phosphatase 2A (PP2A) is the main source of phosphatase activity in the cell, but the molecular details of substrate recognition are unknown. Here, we report that a conserved surface-exposed pocket on PP2A regulatory B56 subunits binds to a consensus sequence on interacting proteins, which we term the LxxIxE motif. The composition of the motif modulates the affinity for B56, which in turn determines the phosphorylation status of associated substrates. Phosphorylation of amino acid residues within the motif increases B56 binding, allowing integration of kinase and phosphatase activity. We identify conserved LxxIxE motifs in essential proteins throughout the eukaryotic domain of life and in human viruses, suggesting that the motifs are required for basic cellular function. Our study provides a molecular description of PP2A binding specificity with broad implications for understanding signaling in eukaryotes.

AB - Dynamic protein phosphorylation is a fundamental mechanism regulating biological processes in all organisms. Protein phosphatase 2A (PP2A) is the main source of phosphatase activity in the cell, but the molecular details of substrate recognition are unknown. Here, we report that a conserved surface-exposed pocket on PP2A regulatory B56 subunits binds to a consensus sequence on interacting proteins, which we term the LxxIxE motif. The composition of the motif modulates the affinity for B56, which in turn determines the phosphorylation status of associated substrates. Phosphorylation of amino acid residues within the motif increases B56 binding, allowing integration of kinase and phosphatase activity. We identify conserved LxxIxE motifs in essential proteins throughout the eukaryotic domain of life and in human viruses, suggesting that the motifs are required for basic cellular function. Our study provides a molecular description of PP2A binding specificity with broad implications for understanding signaling in eukaryotes.

U2 - 10.1016/j.molcel.2016.06.024

DO - 10.1016/j.molcel.2016.06.024

M3 - Journal article

C2 - 27453045

VL - 63

SP - 686

EP - 695

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -

ID: 164182539