Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome

Satu Kärkkäinen, Marita Hiipakka, Jing-Huan Wang, Iivari Kleino, Marika Vähä-Jaakkola, G. Herman Renkema, Michael Liss, Ralf Wagner, Kalle Saksela

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    Kuvaus

    We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector. This provided a powerful and unbiased system for simultaneous assaying of the complete human SH3 proteome for the strongest binding to target proteins of interest, without the limitations posed by short linear peptide ligands or confounding variables of more indirect methods for protein interaction screening. Studies involving three ligand proteins, human immunodeficiency virus-1 Nef, p21-activated kinase (PAK) 2 and ADAM15, showed previously reported as well as novel SH3 partners with nanomolar affinities specific for them. This argues that SH3 domains may have a more dominant role in directing cellular protein interactions than has been assumed. Besides showing potentially important new SH3-directed interactions, these studies also led to the discovery of novel signalling proteins, such as the PAK2-binding adaptor protein POSH2 and the ADAM15-binding sorting nexin family member SNX30.
    Alkuperäiskielienglanti
    LehtiEMBO Reports
    Vuosikerta7
    Numero2
    Sivut186-191
    Sivumäärä6
    ISSN1469-221X
    DOI - pysyväislinkit
    TilaJulkaistu - 2006
    OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

    Lainaa tätä

    Kärkkäinen, Satu ; Hiipakka, Marita ; Wang, Jing-Huan ; Kleino, Iivari ; Vähä-Jaakkola, Marika ; Renkema, G. Herman ; Liss, Michael ; Wagner, Ralf ; Saksela, Kalle. / Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome. Julkaisussa: EMBO Reports. 2006 ; Vuosikerta 7, Nro 2. Sivut 186-191.
    @article{41eba693fede448b9c4104326d619253,
    title = "Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome",
    abstract = "We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector. This provided a powerful and unbiased system for simultaneous assaying of the complete human SH3 proteome for the strongest binding to target proteins of interest, without the limitations posed by short linear peptide ligands or confounding variables of more indirect methods for protein interaction screening. Studies involving three ligand proteins, human immunodeficiency virus-1 Nef, p21-activated kinase (PAK) 2 and ADAM15, showed previously reported as well as novel SH3 partners with nanomolar affinities specific for them. This argues that SH3 domains may have a more dominant role in directing cellular protein interactions than has been assumed. Besides showing potentially important new SH3-directed interactions, these studies also led to the discovery of novel signalling proteins, such as the PAK2-binding adaptor protein POSH2 and the ADAM15-binding sorting nexin family member SNX30.",
    author = "Satu K{\"a}rkk{\"a}inen and Marita Hiipakka and Jing-Huan Wang and Iivari Kleino and Marika V{\"a}h{\"a}-Jaakkola and Renkema, {G. Herman} and Michael Liss and Ralf Wagner and Kalle Saksela",
    year = "2006",
    doi = "10.1038/sj.embor.7400596",
    language = "English",
    volume = "7",
    pages = "186--191",
    journal = "EMBO Reports",
    issn = "1469-221X",
    publisher = "Wiley",
    number = "2",

    }

    Kärkkäinen, S, Hiipakka, M, Wang, J-H, Kleino, I, Vähä-Jaakkola, M, Renkema, GH, Liss, M, Wagner, R & Saksela, K 2006, 'Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome', EMBO Reports, Vuosikerta 7, Nro 2, Sivut 186-191. https://doi.org/10.1038/sj.embor.7400596

    Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome. / Kärkkäinen, Satu; Hiipakka, Marita; Wang, Jing-Huan; Kleino, Iivari; Vähä-Jaakkola, Marika; Renkema, G. Herman; Liss, Michael; Wagner, Ralf; Saksela, Kalle.

    julkaisussa: EMBO Reports, Vuosikerta 7, Nro 2, 2006, s. 186-191.

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    TY - JOUR

    T1 - Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome

    AU - Kärkkäinen, Satu

    AU - Hiipakka, Marita

    AU - Wang, Jing-Huan

    AU - Kleino, Iivari

    AU - Vähä-Jaakkola, Marika

    AU - Renkema, G. Herman

    AU - Liss, Michael

    AU - Wagner, Ralf

    AU - Saksela, Kalle

    PY - 2006

    Y1 - 2006

    N2 - We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector. This provided a powerful and unbiased system for simultaneous assaying of the complete human SH3 proteome for the strongest binding to target proteins of interest, without the limitations posed by short linear peptide ligands or confounding variables of more indirect methods for protein interaction screening. Studies involving three ligand proteins, human immunodeficiency virus-1 Nef, p21-activated kinase (PAK) 2 and ADAM15, showed previously reported as well as novel SH3 partners with nanomolar affinities specific for them. This argues that SH3 domains may have a more dominant role in directing cellular protein interactions than has been assumed. Besides showing potentially important new SH3-directed interactions, these studies also led to the discovery of novel signalling proteins, such as the PAK2-binding adaptor protein POSH2 and the ADAM15-binding sorting nexin family member SNX30.

    AB - We have determined the human genome to contain 296 different Src homology-3 (SH3) domains and cloned them into a phage-display vector. This provided a powerful and unbiased system for simultaneous assaying of the complete human SH3 proteome for the strongest binding to target proteins of interest, without the limitations posed by short linear peptide ligands or confounding variables of more indirect methods for protein interaction screening. Studies involving three ligand proteins, human immunodeficiency virus-1 Nef, p21-activated kinase (PAK) 2 and ADAM15, showed previously reported as well as novel SH3 partners with nanomolar affinities specific for them. This argues that SH3 domains may have a more dominant role in directing cellular protein interactions than has been assumed. Besides showing potentially important new SH3-directed interactions, these studies also led to the discovery of novel signalling proteins, such as the PAK2-binding adaptor protein POSH2 and the ADAM15-binding sorting nexin family member SNX30.

    U2 - 10.1038/sj.embor.7400596

    DO - 10.1038/sj.embor.7400596

    M3 - Article

    VL - 7

    SP - 186

    EP - 191

    JO - EMBO Reports

    JF - EMBO Reports

    SN - 1469-221X

    IS - 2

    ER -