Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression

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Standard

Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression. / Kruse, Thomas; Zhang, Gang; Larsen, Marie Sofie Yoo; Lischetti, Tiziana; Streicher, Werner; Nielsen, Tine Kragh; Bjørn, Sara Petersen; Nilsson, Jakob.

In: Journal of Cell Science, Vol. 126, 23.01.2013, p. 1086-1092.

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

Harvard

Kruse, T, Zhang, G, Larsen, MSY, Lischetti, T, Streicher, W, Nielsen, TK, Bjørn, SP & Nilsson, J 2013, 'Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression', Journal of Cell Science, vol. 126, pp. 1086-1092. https://doi.org/10.1242/jcs.122481

APA

Kruse, T., Zhang, G., Larsen, M. S. Y., Lischetti, T., Streicher, W., Nielsen, T. K., Bjørn, S. P., & Nilsson, J. (2013). Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression. Journal of Cell Science, 126, 1086-1092. https://doi.org/10.1242/jcs.122481

Vancouver

Kruse T, Zhang G, Larsen MSY, Lischetti T, Streicher W, Nielsen TK et al. Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression. Journal of Cell Science. 2013 Jan 23;126:1086-1092. https://doi.org/10.1242/jcs.122481

Author

Kruse, Thomas ; Zhang, Gang ; Larsen, Marie Sofie Yoo ; Lischetti, Tiziana ; Streicher, Werner ; Nielsen, Tine Kragh ; Bjørn, Sara Petersen ; Nilsson, Jakob. / Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression. In: Journal of Cell Science. 2013 ; Vol. 126. pp. 1086-1092.

Bibtex

@article{eec316772a5c45afae0fce840582ebbb,
title = "Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression",
abstract = "BubR1 is a central component of the spindle assembly checkpoint (SAC) that inhibits progression into anaphase in response to improper kinetochore-microtubule interactions. In addition BubR1 also helps stabilize kinetochore-microtubule interactions by counteracting the Aurora B kinase but the mechanism behind this is not clear. Here we show that BubR1 directly binds to the B56 family of PP2A regulatory subunits through a conserved motif that is phosphorylated by Cdk1 and Plk1. Two highly conserved hydrophobic residues surrounding the S670 Cdk1 phosphorylation site are required for B56 binding and mutation of these residues prevents the establishment of a proper metaphase plate and delays cells in mitosis. Furthermore, we show that phosphorylation of S670 and S676 stimulates the binding of B56 to BubR1 and that BubR1 targets a pool of B56 to kinetochores. Our data suggests that BubR1 counteracts Aurora B kinase activity at improperly attached kinetochores by recruiting B56-PP2A phosphatase complexes.",
author = "Thomas Kruse and Gang Zhang and Larsen, {Marie Sofie Yoo} and Tiziana Lischetti and Werner Streicher and Nielsen, {Tine Kragh} and Bj{\o}rn, {Sara Petersen} and Jakob Nilsson",
year = "2013",
month = jan,
day = "23",
doi = "10.1242/jcs.122481",
language = "English",
volume = "126",
pages = "1086--1092",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",

}

RIS

TY - JOUR

T1 - Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression

AU - Kruse, Thomas

AU - Zhang, Gang

AU - Larsen, Marie Sofie Yoo

AU - Lischetti, Tiziana

AU - Streicher, Werner

AU - Nielsen, Tine Kragh

AU - Bjørn, Sara Petersen

AU - Nilsson, Jakob

PY - 2013/1/23

Y1 - 2013/1/23

N2 - BubR1 is a central component of the spindle assembly checkpoint (SAC) that inhibits progression into anaphase in response to improper kinetochore-microtubule interactions. In addition BubR1 also helps stabilize kinetochore-microtubule interactions by counteracting the Aurora B kinase but the mechanism behind this is not clear. Here we show that BubR1 directly binds to the B56 family of PP2A regulatory subunits through a conserved motif that is phosphorylated by Cdk1 and Plk1. Two highly conserved hydrophobic residues surrounding the S670 Cdk1 phosphorylation site are required for B56 binding and mutation of these residues prevents the establishment of a proper metaphase plate and delays cells in mitosis. Furthermore, we show that phosphorylation of S670 and S676 stimulates the binding of B56 to BubR1 and that BubR1 targets a pool of B56 to kinetochores. Our data suggests that BubR1 counteracts Aurora B kinase activity at improperly attached kinetochores by recruiting B56-PP2A phosphatase complexes.

AB - BubR1 is a central component of the spindle assembly checkpoint (SAC) that inhibits progression into anaphase in response to improper kinetochore-microtubule interactions. In addition BubR1 also helps stabilize kinetochore-microtubule interactions by counteracting the Aurora B kinase but the mechanism behind this is not clear. Here we show that BubR1 directly binds to the B56 family of PP2A regulatory subunits through a conserved motif that is phosphorylated by Cdk1 and Plk1. Two highly conserved hydrophobic residues surrounding the S670 Cdk1 phosphorylation site are required for B56 binding and mutation of these residues prevents the establishment of a proper metaphase plate and delays cells in mitosis. Furthermore, we show that phosphorylation of S670 and S676 stimulates the binding of B56 to BubR1 and that BubR1 targets a pool of B56 to kinetochores. Our data suggests that BubR1 counteracts Aurora B kinase activity at improperly attached kinetochores by recruiting B56-PP2A phosphatase complexes.

U2 - 10.1242/jcs.122481

DO - 10.1242/jcs.122481

M3 - Journal article

C2 - 23345399

VL - 126

SP - 1086

EP - 1092

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

ER -

ID: 45106279