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  1. Artikel ; Online: ArreSTick motif controls β-arrestin-binding stability and extends phosphorylation-dependent β-arrestin interactions to non-receptor proteins.

    Tóth, András Dávid / Soltész-Katona, Eszter / Kis, Katalin / Guti, Viktor / Gilzer, Sharon / Prokop, Susanne / Boros, Roxána / Misák, Ádám / Balla, András / Várnai, Péter / Turiák, Lilla / Ács, András / Drahos, László / Inoue, Asuka / Hunyady, László / Turu, Gábor

    Cell reports

    2024  Band 43, Heft 5, Seite(n) 114241

    Abstract: The binding and function of β-arrestins are regulated by specific phosphorylation motifs present in G protein-coupled receptors (GPCRs). However, the exact arrangement of phosphorylated amino acids responsible for establishing a stable interaction ... ...

    Abstract The binding and function of β-arrestins are regulated by specific phosphorylation motifs present in G protein-coupled receptors (GPCRs). However, the exact arrangement of phosphorylated amino acids responsible for establishing a stable interaction remains unclear. We employ a 1D sequence convolution model trained on GPCRs with established β-arrestin-binding properties. With this approach, amino acid motifs characteristic of GPCRs that form stable interactions with β-arrestins can be identified, a pattern that we name "arreSTick." Intriguingly, the arreSTick pattern is also present in numerous non-receptor proteins. Using proximity biotinylation assay and mass spectrometry analysis, we demonstrate that the arreSTick motif controls the interaction between many non-receptor proteins and β-arrestin2. The HIV-1 Tat-specific factor 1 (HTSF1 or HTATSF1), a nuclear transcription factor, contains the arreSTick pattern, and its subcellular localization is influenced by β-arrestin2. Our findings unveil a broader role for β-arrestins in phosphorylation-dependent interactions, extending beyond GPCRs to encompass non-receptor proteins as well.
    Mesh-Begriff(e) Phosphorylation ; Humans ; beta-Arrestins/metabolism ; Protein Binding ; Amino Acid Motifs ; HEK293 Cells ; beta-Arrestin 2/metabolism ; Amino Acid Sequence ; Protein Stability
    Chemische Substanzen beta-Arrestins ; beta-Arrestin 2
    Sprache Englisch
    Erscheinungsdatum 2024-05-17
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2024.114241
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Biased Coupling to β-Arrestin of Two Common Variants of the CB

    Turu, Gábor / Soltész-Katona, Eszter / Tóth, András Dávid / Juhász, Cintia / Cserző, Miklós / Misák, Ádám / Balla, András / Caron, Marc G / Hunyady, László

    Frontiers in endocrinology

    2021  Band 12, Seite(n) 714561

    Abstract: β-arrestins are partners of the G protein-coupled receptors (GPCRs), regulating their intracellular trafficking and signaling. Development of biased GPCR agonists, selectively targeting either G protein or β-arrestin pathways, are in the focus of ... ...

    Abstract β-arrestins are partners of the G protein-coupled receptors (GPCRs), regulating their intracellular trafficking and signaling. Development of biased GPCR agonists, selectively targeting either G protein or β-arrestin pathways, are in the focus of interest due to their therapeutic potential in different pathological conditions. The CB
    Mesh-Begriff(e) HEK293 Cells ; Humans ; Mutation, Missense ; Protein Binding ; Protein Transport ; Receptor, Cannabinoid, CB2/chemistry ; Receptor, Cannabinoid, CB2/genetics ; Receptor, Cannabinoid, CB2/metabolism ; beta-Arrestins/genetics ; beta-Arrestins/metabolism
    Chemische Substanzen Receptor, Cannabinoid, CB2 ; beta-Arrestins
    Sprache Englisch
    Erscheinungsdatum 2021-08-16
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2021.714561
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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