Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

Markus Posch; Guennadi A. Khoudoli; Sam Swift; Emma M. King; Jennifer G. DeLuca; Jason R. Swedlow

doi:10.1083/jcb.200912046

Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

Markus Posch, Guennadi A. Khoudoli, Sam Swift, Emma M. King, Jennifer G. DeLuca, Jason R. Swedlow (Lead / Corresponding author)

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Abstract

We have studied Sds22, a conserved regulator of protein phosphatase 1 (PP1) activity, and determined its role in modulating the activity of aurora B kinase and kinetochore-microtubule inter-actions. Sds22 is required for proper progression through mitosis and localization of PP1 to mitotic kinetochores. Depletion of Sds22 increases aurora B T-loop phosphorylation and the rate of recovery from monastrol arrest. Phospho-aurora B accumulates at kinetochores in Sds22-depleted cells juxtaposed to critical kinetochore substrates. Sds22 modulates sister kinetochore distance and the interaction between Hec1 and the microtubule lattice and, thus, the activation of the spindle assembly checkpoint. These results demonstrate that Sds22 specifically defines PP1 function and localization in mitosis. Sds22 regulates PP1 targeting to the kinetochore, accumulation of phospho-aurora B, and force generation at the kinetochore-microtubule interface.

Original language	English
Pages (from-to)	61-74
Number of pages	14
Journal	Journal of Cell Biology
Volume	191
Issue number	1
DOIs	https://doi.org/10.1083/jcb.200912046
Publication status	Published - 4 Oct 2010

Keywords

HISTONE H3 PHOSPHORYLATION
STRUCTURED ILLUMINATION MICROSCOPY
LIFETIME IMAGING MICROSCOPY
PROTEIN PHOSPHATASE 1
CHROMOSOME SEGREGATION
ESSENTIAL ROLES
CELL-DIVISION
KINASE
SPINDLE
YEAST

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title = "Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis",

abstract = "We have studied Sds22, a conserved regulator of protein phosphatase 1 (PP1) activity, and determined its role in modulating the activity of aurora B kinase and kinetochore-microtubule inter-actions. Sds22 is required for proper progression through mitosis and localization of PP1 to mitotic kinetochores. Depletion of Sds22 increases aurora B T-loop phosphorylation and the rate of recovery from monastrol arrest. Phospho-aurora B accumulates at kinetochores in Sds22-depleted cells juxtaposed to critical kinetochore substrates. Sds22 modulates sister kinetochore distance and the interaction between Hec1 and the microtubule lattice and, thus, the activation of the spindle assembly checkpoint. These results demonstrate that Sds22 specifically defines PP1 function and localization in mitosis. Sds22 regulates PP1 targeting to the kinetochore, accumulation of phospho-aurora B, and force generation at the kinetochore-microtubule interface.",

keywords = "HISTONE H3 PHOSPHORYLATION, STRUCTURED ILLUMINATION MICROSCOPY, LIFETIME IMAGING MICROSCOPY, PROTEIN PHOSPHATASE 1, CHROMOSOME SEGREGATION, ESSENTIAL ROLES, CELL-DIVISION, KINASE, SPINDLE, YEAST",

author = "Markus Posch and Khoudoli, {Guennadi A.} and Sam Swift and King, {Emma M.} and DeLuca, {Jennifer G.} and Swedlow, {Jason R.}",

year = "2010",

month = oct,

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doi = "10.1083/jcb.200912046",

language = "English",

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AU - Posch, Markus

AU - Khoudoli, Guennadi A.

AU - Swift, Sam

AU - King, Emma M.

AU - DeLuca, Jennifer G.

AU - Swedlow, Jason R.

PY - 2010/10/4

Y1 - 2010/10/4

N2 - We have studied Sds22, a conserved regulator of protein phosphatase 1 (PP1) activity, and determined its role in modulating the activity of aurora B kinase and kinetochore-microtubule inter-actions. Sds22 is required for proper progression through mitosis and localization of PP1 to mitotic kinetochores. Depletion of Sds22 increases aurora B T-loop phosphorylation and the rate of recovery from monastrol arrest. Phospho-aurora B accumulates at kinetochores in Sds22-depleted cells juxtaposed to critical kinetochore substrates. Sds22 modulates sister kinetochore distance and the interaction between Hec1 and the microtubule lattice and, thus, the activation of the spindle assembly checkpoint. These results demonstrate that Sds22 specifically defines PP1 function and localization in mitosis. Sds22 regulates PP1 targeting to the kinetochore, accumulation of phospho-aurora B, and force generation at the kinetochore-microtubule interface.

AB - We have studied Sds22, a conserved regulator of protein phosphatase 1 (PP1) activity, and determined its role in modulating the activity of aurora B kinase and kinetochore-microtubule inter-actions. Sds22 is required for proper progression through mitosis and localization of PP1 to mitotic kinetochores. Depletion of Sds22 increases aurora B T-loop phosphorylation and the rate of recovery from monastrol arrest. Phospho-aurora B accumulates at kinetochores in Sds22-depleted cells juxtaposed to critical kinetochore substrates. Sds22 modulates sister kinetochore distance and the interaction between Hec1 and the microtubule lattice and, thus, the activation of the spindle assembly checkpoint. These results demonstrate that Sds22 specifically defines PP1 function and localization in mitosis. Sds22 regulates PP1 targeting to the kinetochore, accumulation of phospho-aurora B, and force generation at the kinetochore-microtubule interface.

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KW - STRUCTURED ILLUMINATION MICROSCOPY

KW - LIFETIME IMAGING MICROSCOPY

KW - PROTEIN PHOSPHATASE 1

KW - CHROMOSOME SEGREGATION

KW - ESSENTIAL ROLES

KW - CELL-DIVISION

KW - KINASE

KW - SPINDLE

KW - YEAST

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DO - 10.1083/jcb.200912046

M3 - Article

C2 - 20921135

SN - 0021-9525

VL - 191

SP - 61

EP - 74

JO - Journal of Cell Biology

JF - Journal of Cell Biology

IS - 1

ER -

Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

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Keywords

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Aref#d: 19770. Division of Gene Regulation and Expression Strategic Award

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Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

Abstract

Keywords

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Aref#d: 19770. Division of Gene Regulation and Expression Strategic Award

Cite this