A phosphoproteomics approach to elucidate neuropeptide signal transduction controlling insect metamorphosis

Kim Rewitz, Martin Røssel Larsen, Anders Løbner-Olesen, Robert Rybczynski, Michael B. O'Connor, Lawrence Gilbert

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

    Resumé

    In insects, the neuropeptide prothoracicotropic hormone (PTTH) stimulates production of ecdysone (E) in the prothoracic glands (PGs). E is the precursor of the principal steroid hormone, 20-hydroxyecdysone (20E). that is responsible for eliciting molting and metamorphosis. In this study, we used quantitative phosphoproteomics to investigate signal transduction events initiated by PTTH. We identified Spook (CYP307A1), a suspected rate-limiting enzyme for E biosynthesis, and components of the mitogen-activated protein kinase (MAPK) pathway, as major phosphorylation targets of PTTH signaling. Further, proteins not previously linked to PTTH and ecdysone biosynthesis were identified as targets of PTTH signaling. These include proteins involved in signal transduction, endosomal trafficking, constituents of the cytoskeleton and regulators of transcription and translation. Our screen shows that PTTH likely stimulates E production by activation of Spook, an integral enzyme in the E biosynthetic pathway. This directly connects PTTH signaling to the pathway that produces E. A new mechanism for regulation of E biosynthesis in insects is proposed. (C) 2009 Elsevier Ltd. All rights reserved.
    OriginalsprogEngelsk
    TidsskriftInsect Biochemistry and Molecular Biology
    Vol/bind39
    Udgave nummer7
    Sider (fra-til)475-483
    ISSN0965-1748
    DOI
    StatusUdgivet - 2009

    Citer dette

    Rewitz, Kim ; Larsen, Martin Røssel ; Løbner-Olesen, Anders ; Rybczynski, Robert ; O'Connor, Michael B. ; Gilbert, Lawrence. / A phosphoproteomics approach to elucidate neuropeptide signal transduction controlling insect metamorphosis. I: Insect Biochemistry and Molecular Biology. 2009 ; Bind 39, Nr. 7. s. 475-483.
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    title = "A phosphoproteomics approach to elucidate neuropeptide signal transduction controlling insect metamorphosis",
    abstract = "In insects, the neuropeptide prothoracicotropic hormone (PTTH) stimulates production of ecdysone (E) in the prothoracic glands (PGs). E is the precursor of the principal steroid hormone, 20-hydroxyecdysone (20E). that is responsible for eliciting molting and metamorphosis. In this study, we used quantitative phosphoproteomics to investigate signal transduction events initiated by PTTH. We identified Spook (CYP307A1), a suspected rate-limiting enzyme for E biosynthesis, and components of the mitogen-activated protein kinase (MAPK) pathway, as major phosphorylation targets of PTTH signaling. Further, proteins not previously linked to PTTH and ecdysone biosynthesis were identified as targets of PTTH signaling. These include proteins involved in signal transduction, endosomal trafficking, constituents of the cytoskeleton and regulators of transcription and translation. Our screen shows that PTTH likely stimulates E production by activation of Spook, an integral enzyme in the E biosynthetic pathway. This directly connects PTTH signaling to the pathway that produces E. A new mechanism for regulation of E biosynthesis in insects is proposed. (C) 2009 Elsevier Ltd. All rights reserved.",
    keywords = "20-hydroxyecdysone, PTTH, Phosphoproteomics, Spook, Titanium dioxide, SIMAC",
    author = "Kim Rewitz and Larsen, {Martin R{\o}ssel} and Anders L{\o}bner-Olesen and Robert Rybczynski and O'Connor, {Michael B.} and Lawrence Gilbert",
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    A phosphoproteomics approach to elucidate neuropeptide signal transduction controlling insect metamorphosis. / Rewitz, Kim; Larsen, Martin Røssel; Løbner-Olesen, Anders; Rybczynski, Robert; O'Connor, Michael B.; Gilbert, Lawrence.

    I: Insect Biochemistry and Molecular Biology, Bind 39, Nr. 7, 2009, s. 475-483.

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

    TY - JOUR

    T1 - A phosphoproteomics approach to elucidate neuropeptide signal transduction controlling insect metamorphosis

    AU - Rewitz, Kim

    AU - Larsen, Martin Røssel

    AU - Løbner-Olesen, Anders

    AU - Rybczynski, Robert

    AU - O'Connor, Michael B.

    AU - Gilbert, Lawrence

    PY - 2009

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    N2 - In insects, the neuropeptide prothoracicotropic hormone (PTTH) stimulates production of ecdysone (E) in the prothoracic glands (PGs). E is the precursor of the principal steroid hormone, 20-hydroxyecdysone (20E). that is responsible for eliciting molting and metamorphosis. In this study, we used quantitative phosphoproteomics to investigate signal transduction events initiated by PTTH. We identified Spook (CYP307A1), a suspected rate-limiting enzyme for E biosynthesis, and components of the mitogen-activated protein kinase (MAPK) pathway, as major phosphorylation targets of PTTH signaling. Further, proteins not previously linked to PTTH and ecdysone biosynthesis were identified as targets of PTTH signaling. These include proteins involved in signal transduction, endosomal trafficking, constituents of the cytoskeleton and regulators of transcription and translation. Our screen shows that PTTH likely stimulates E production by activation of Spook, an integral enzyme in the E biosynthetic pathway. This directly connects PTTH signaling to the pathway that produces E. A new mechanism for regulation of E biosynthesis in insects is proposed. (C) 2009 Elsevier Ltd. All rights reserved.

    AB - In insects, the neuropeptide prothoracicotropic hormone (PTTH) stimulates production of ecdysone (E) in the prothoracic glands (PGs). E is the precursor of the principal steroid hormone, 20-hydroxyecdysone (20E). that is responsible for eliciting molting and metamorphosis. In this study, we used quantitative phosphoproteomics to investigate signal transduction events initiated by PTTH. We identified Spook (CYP307A1), a suspected rate-limiting enzyme for E biosynthesis, and components of the mitogen-activated protein kinase (MAPK) pathway, as major phosphorylation targets of PTTH signaling. Further, proteins not previously linked to PTTH and ecdysone biosynthesis were identified as targets of PTTH signaling. These include proteins involved in signal transduction, endosomal trafficking, constituents of the cytoskeleton and regulators of transcription and translation. Our screen shows that PTTH likely stimulates E production by activation of Spook, an integral enzyme in the E biosynthetic pathway. This directly connects PTTH signaling to the pathway that produces E. A new mechanism for regulation of E biosynthesis in insects is proposed. (C) 2009 Elsevier Ltd. All rights reserved.

    KW - 20-hydroxyecdysone

    KW - PTTH

    KW - Phosphoproteomics

    KW - Spook

    KW - Titanium dioxide

    KW - SIMAC

    U2 - 10.1016/j.ibmb.2009.04.005

    DO - 10.1016/j.ibmb.2009.04.005

    M3 - Journal article

    VL - 39

    SP - 475

    EP - 483

    JO - Insect Biochemistry and Molecular Biology

    JF - Insect Biochemistry and Molecular Biology

    SN - 0965-1748

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    ER -