Bod1 regulates protein phosphatase 2A at mitotic kinetochores

Iain Porter, Katharina Schleicher, Michael Porter, Jason Swedlow (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    39 Citations (Scopus)

    Abstract

    Mitotic entry and progression require the activation of several mitotic kinases and the proper regulation and localization of several phosphatases. The activity and localization of each of these enzymes is tightly controlled through a series of specific activators, inhibitors and regulatory subunits. Two proteins, Ensa and Arpp-19, were recently identified as specific inhibitors of PP2A-B55 and are critical for allowing full activity of Cdk1/cyclin B and entry into mitosis. Here we show that Bod1, a protein required for proper chromosome alignment at mitosis, shares sequence similarity with Ensa and Arpp-19 and specifically inhibits the kinetochore-associated PP2A-B56 holoenzyme. PP2A-B56 regulates the stability of kinetochore-microtubule attachments by dephosphorylating several kinetochore proteins. Loss of Bod1 changes the balance of phosphorylation at kinetochores, causing defects in kinetochore function. Bod1, Ensa and Arpp-19 define a family of specific PP2A inhibitors that regulate specific PP2A holoenzymes at distinct locations and points in the cell cycle.
    Original languageEnglish
    Article number2677
    JournalNature Communications
    Volume4
    DOIs
    Publication statusPublished - 25 Oct 2013

    Fingerprint

    Kinetochores
    Protein Phosphatase 2
    phosphatases
    inhibitors
    mitosis
    Holoenzymes
    proteins
    entry
    Cyclin B
    phosphorylation
    Phosphorylation
    Proteins
    Mitosis
    chromosomes
    Chromosomes
    Phosphoric Monoester Hydrolases
    progressions
    attachment
    enzymes
    Phosphotransferases

    Cite this

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    title = "Bod1 regulates protein phosphatase 2A at mitotic kinetochores",
    abstract = "Mitotic entry and progression require the activation of several mitotic kinases and the proper regulation and localization of several phosphatases. The activity and localization of each of these enzymes is tightly controlled through a series of specific activators, inhibitors and regulatory subunits. Two proteins, Ensa and Arpp-19, were recently identified as specific inhibitors of PP2A-B55 and are critical for allowing full activity of Cdk1/cyclin B and entry into mitosis. Here we show that Bod1, a protein required for proper chromosome alignment at mitosis, shares sequence similarity with Ensa and Arpp-19 and specifically inhibits the kinetochore-associated PP2A-B56 holoenzyme. PP2A-B56 regulates the stability of kinetochore-microtubule attachments by dephosphorylating several kinetochore proteins. Loss of Bod1 changes the balance of phosphorylation at kinetochores, causing defects in kinetochore function. Bod1, Ensa and Arpp-19 define a family of specific PP2A inhibitors that regulate specific PP2A holoenzymes at distinct locations and points in the cell cycle.",
    author = "Iain Porter and Katharina Schleicher and Michael Porter and Jason Swedlow",
    year = "2013",
    month = "10",
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    doi = "10.1038/ncomms3677",
    language = "English",
    volume = "4",
    journal = "Nature Communications",
    issn = "2041-1723",
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    Bod1 regulates protein phosphatase 2A at mitotic kinetochores. / Porter, Iain; Schleicher, Katharina; Porter, Michael; Swedlow, Jason (Lead / Corresponding author).

    In: Nature Communications, Vol. 4, 2677, 25.10.2013.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Bod1 regulates protein phosphatase 2A at mitotic kinetochores

    AU - Porter, Iain

    AU - Schleicher, Katharina

    AU - Porter, Michael

    AU - Swedlow, Jason

    PY - 2013/10/25

    Y1 - 2013/10/25

    N2 - Mitotic entry and progression require the activation of several mitotic kinases and the proper regulation and localization of several phosphatases. The activity and localization of each of these enzymes is tightly controlled through a series of specific activators, inhibitors and regulatory subunits. Two proteins, Ensa and Arpp-19, were recently identified as specific inhibitors of PP2A-B55 and are critical for allowing full activity of Cdk1/cyclin B and entry into mitosis. Here we show that Bod1, a protein required for proper chromosome alignment at mitosis, shares sequence similarity with Ensa and Arpp-19 and specifically inhibits the kinetochore-associated PP2A-B56 holoenzyme. PP2A-B56 regulates the stability of kinetochore-microtubule attachments by dephosphorylating several kinetochore proteins. Loss of Bod1 changes the balance of phosphorylation at kinetochores, causing defects in kinetochore function. Bod1, Ensa and Arpp-19 define a family of specific PP2A inhibitors that regulate specific PP2A holoenzymes at distinct locations and points in the cell cycle.

    AB - Mitotic entry and progression require the activation of several mitotic kinases and the proper regulation and localization of several phosphatases. The activity and localization of each of these enzymes is tightly controlled through a series of specific activators, inhibitors and regulatory subunits. Two proteins, Ensa and Arpp-19, were recently identified as specific inhibitors of PP2A-B55 and are critical for allowing full activity of Cdk1/cyclin B and entry into mitosis. Here we show that Bod1, a protein required for proper chromosome alignment at mitosis, shares sequence similarity with Ensa and Arpp-19 and specifically inhibits the kinetochore-associated PP2A-B56 holoenzyme. PP2A-B56 regulates the stability of kinetochore-microtubule attachments by dephosphorylating several kinetochore proteins. Loss of Bod1 changes the balance of phosphorylation at kinetochores, causing defects in kinetochore function. Bod1, Ensa and Arpp-19 define a family of specific PP2A inhibitors that regulate specific PP2A holoenzymes at distinct locations and points in the cell cycle.

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