Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules

Yusuke Mori, Yuki Taniyama, Sayori Tanaka, Hiroki Fukuchi, Yasuhiko Terada

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    CDK5RAP2 is a centrosomal protein that regulates the recruitment of a γ-tubulin ring complex (γ-TuRC) onto centrosomes and microtubules (MTs) dynamics as a member of MT plus-end-tracking proteins (+TIPs). In our previous report, we found mammalian Cep169 as a CDK5RAP2 binding partner, and Cep169 accumulates at the distal ends of MTs and centrosomes, and coincides with CDK5RAP2. Depletion of Cep169 induces MT depolymerization, indicating that Cep169 targets MT tips and regulates stability and dynamics of MTs. However, how Cep169 contributes to the stabilization of MT remains unclear. Here we show that Cep169 is able to stabilize MTs and induces formation of long MT bundles with intense acetylation of MTs with CDK5RAP2, when expressed at higher levels in U2OS cells. In addition, we demonstrated that Cep169 forms homodimers through its N-terminal domain and directly interacts with MTs through its C-terminal domain. Interestingly, Cep169 mutants, which lack each domains, completely abolished the activity, respectively. Therefore, Cep169 bundles MTs and induces solid structure of MTs by crosslinking each adjacent MTs as a homodimer.

    Original languageEnglish
    Pages (from-to)754-759
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume467
    Issue number4
    DOIs
    Publication statusPublished - 2015 Nov 27

    Fingerprint

    Microtubules
    Acetylation
    Depolymerization
    Tubulin
    Crosslinking
    Proteins
    Stabilization
    Centrosome

    Keywords

    • +TIPs
    • CDK5RAP2
    • Centrosome
    • MAPs
    • Microtubule bundle

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Cell Biology
    • Molecular Biology

    Cite this

    Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules. / Mori, Yusuke; Taniyama, Yuki; Tanaka, Sayori; Fukuchi, Hiroki; Terada, Yasuhiko.

    In: Biochemical and Biophysical Research Communications, Vol. 467, No. 4, 27.11.2015, p. 754-759.

    Research output: Contribution to journalArticle

    Mori, Yusuke ; Taniyama, Yuki ; Tanaka, Sayori ; Fukuchi, Hiroki ; Terada, Yasuhiko. / Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules. In: Biochemical and Biophysical Research Communications. 2015 ; Vol. 467, No. 4. pp. 754-759.
    @article{dfe049a7e7c543409e5cc44e835daf9e,
    title = "Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules",
    abstract = "CDK5RAP2 is a centrosomal protein that regulates the recruitment of a γ-tubulin ring complex (γ-TuRC) onto centrosomes and microtubules (MTs) dynamics as a member of MT plus-end-tracking proteins (+TIPs). In our previous report, we found mammalian Cep169 as a CDK5RAP2 binding partner, and Cep169 accumulates at the distal ends of MTs and centrosomes, and coincides with CDK5RAP2. Depletion of Cep169 induces MT depolymerization, indicating that Cep169 targets MT tips and regulates stability and dynamics of MTs. However, how Cep169 contributes to the stabilization of MT remains unclear. Here we show that Cep169 is able to stabilize MTs and induces formation of long MT bundles with intense acetylation of MTs with CDK5RAP2, when expressed at higher levels in U2OS cells. In addition, we demonstrated that Cep169 forms homodimers through its N-terminal domain and directly interacts with MTs through its C-terminal domain. Interestingly, Cep169 mutants, which lack each domains, completely abolished the activity, respectively. Therefore, Cep169 bundles MTs and induces solid structure of MTs by crosslinking each adjacent MTs as a homodimer.",
    keywords = "+TIPs, CDK5RAP2, Centrosome, MAPs, Microtubule bundle",
    author = "Yusuke Mori and Yuki Taniyama and Sayori Tanaka and Hiroki Fukuchi and Yasuhiko Terada",
    year = "2015",
    month = "11",
    day = "27",
    doi = "10.1016/j.bbrc.2015.10.069",
    language = "English",
    volume = "467",
    pages = "754--759",
    journal = "Biochemical and Biophysical Research Communications",
    issn = "0006-291X",
    publisher = "Academic Press Inc.",
    number = "4",

    }

    TY - JOUR

    T1 - Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules

    AU - Mori, Yusuke

    AU - Taniyama, Yuki

    AU - Tanaka, Sayori

    AU - Fukuchi, Hiroki

    AU - Terada, Yasuhiko

    PY - 2015/11/27

    Y1 - 2015/11/27

    N2 - CDK5RAP2 is a centrosomal protein that regulates the recruitment of a γ-tubulin ring complex (γ-TuRC) onto centrosomes and microtubules (MTs) dynamics as a member of MT plus-end-tracking proteins (+TIPs). In our previous report, we found mammalian Cep169 as a CDK5RAP2 binding partner, and Cep169 accumulates at the distal ends of MTs and centrosomes, and coincides with CDK5RAP2. Depletion of Cep169 induces MT depolymerization, indicating that Cep169 targets MT tips and regulates stability and dynamics of MTs. However, how Cep169 contributes to the stabilization of MT remains unclear. Here we show that Cep169 is able to stabilize MTs and induces formation of long MT bundles with intense acetylation of MTs with CDK5RAP2, when expressed at higher levels in U2OS cells. In addition, we demonstrated that Cep169 forms homodimers through its N-terminal domain and directly interacts with MTs through its C-terminal domain. Interestingly, Cep169 mutants, which lack each domains, completely abolished the activity, respectively. Therefore, Cep169 bundles MTs and induces solid structure of MTs by crosslinking each adjacent MTs as a homodimer.

    AB - CDK5RAP2 is a centrosomal protein that regulates the recruitment of a γ-tubulin ring complex (γ-TuRC) onto centrosomes and microtubules (MTs) dynamics as a member of MT plus-end-tracking proteins (+TIPs). In our previous report, we found mammalian Cep169 as a CDK5RAP2 binding partner, and Cep169 accumulates at the distal ends of MTs and centrosomes, and coincides with CDK5RAP2. Depletion of Cep169 induces MT depolymerization, indicating that Cep169 targets MT tips and regulates stability and dynamics of MTs. However, how Cep169 contributes to the stabilization of MT remains unclear. Here we show that Cep169 is able to stabilize MTs and induces formation of long MT bundles with intense acetylation of MTs with CDK5RAP2, when expressed at higher levels in U2OS cells. In addition, we demonstrated that Cep169 forms homodimers through its N-terminal domain and directly interacts with MTs through its C-terminal domain. Interestingly, Cep169 mutants, which lack each domains, completely abolished the activity, respectively. Therefore, Cep169 bundles MTs and induces solid structure of MTs by crosslinking each adjacent MTs as a homodimer.

    KW - +TIPs

    KW - CDK5RAP2

    KW - Centrosome

    KW - MAPs

    KW - Microtubule bundle

    UR - http://www.scopus.com/inward/record.url?scp=84946593175&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84946593175&partnerID=8YFLogxK

    U2 - 10.1016/j.bbrc.2015.10.069

    DO - 10.1016/j.bbrc.2015.10.069

    M3 - Article

    C2 - 26482847

    AN - SCOPUS:84946593175

    VL - 467

    SP - 754

    EP - 759

    JO - Biochemical and Biophysical Research Communications

    JF - Biochemical and Biophysical Research Communications

    SN - 0006-291X

    IS - 4

    ER -