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  1. Article ; Online: Switchable Control of Scaffold Protein Activity via Engineered Phosphoregulated Autoinhibition.

    Hazegh Nikroo, Arjan / Lemmens, Lenne J M / Wezeman, Tim / Ottmann, Christian / Merkx, Maarten / Brunsveld, Luc

    ACS synthetic biology

    2022  Volume 11, Issue 7, Page(s) 2464–2472

    Abstract: Scaffold proteins operate as organizing hubs to enable high-fidelity signaling, fulfilling crucial roles in the regulation of cellular processes. Bottom-up construction of controllable scaffolding platforms is attractive for the implementation of ... ...

    Abstract Scaffold proteins operate as organizing hubs to enable high-fidelity signaling, fulfilling crucial roles in the regulation of cellular processes. Bottom-up construction of controllable scaffolding platforms is attractive for the implementation of regulatory processes in synthetic biology. Here, we present a modular and switchable synthetic scaffolding system, integrating scaffold-mediated signaling with switchable kinase/phosphatase input control. Phosphorylation-responsive inhibitory peptide motifs were fused to 14-3-3 proteins to generate dimeric protein scaffolds with appended regulatory peptide motifs. The availability of the scaffold for intermolecular partner protein binding could be lowered up to 35-fold upon phosphorylation of the autoinhibition motifs, as demonstrated using three different kinases. In addition, a hetero-bivalent autoinhibitory platform design allowed for dual-kinase input regulation of scaffold activity. Reversibility of the regulatory platform was illustrated through phosphatase-controlled abrogation of autoinhibition, resulting in full recovery of 14-3-3 scaffold activity.
    MeSH term(s) 14-3-3 Proteins/chemistry ; Peptides/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Protein Binding
    Chemical Substances 14-3-3 Proteins ; Peptides ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
    Language English
    Publishing date 2022-06-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2161-5063
    ISSN (online) 2161-5063
    DOI 10.1021/acssynbio.2c00122
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Regulating Chemokine-Receptor Interactions through the Site-Specific Bioorthogonal Conjugation of Photoresponsive DNA Strands.

    van Stevendaal, Marleen H M E / Hazegh Nikroo, Arjan / Mason, Alexander F / Jansen, Jitske / Yewdall, N Amy / van Hest, Jan C M

    Bioconjugate chemistry

    2023  Volume 34, Issue 11, Page(s) 2089–2095

    Abstract: Oligonucleotide conjugation has emerged as a versatile molecular tool for regulating protein activity. A state-of-the-art labeling strategy includes the site-specific conjugation of DNA, by employing bioorthogonal groups genetically incorporated in ... ...

    Abstract Oligonucleotide conjugation has emerged as a versatile molecular tool for regulating protein activity. A state-of-the-art labeling strategy includes the site-specific conjugation of DNA, by employing bioorthogonal groups genetically incorporated in proteins through unnatural amino acids (UAAs). The incorporation of UAAs in chemokines has to date, however, remained underexplored, probably due to their sometimes poor stability following recombinant expression. In this work, we designed a fluorescent stromal-derived factor-1β (SDF-1β) chemokine fusion protein with a bioorthogonal functionality amenable for click reactions. Using amber stop codon suppression, p-azido-
    MeSH term(s) Amino Acids/chemistry ; Phenylalanine/chemistry ; Green Fluorescent Proteins/chemistry ; DNA ; Chemokines
    Chemical Substances Amino Acids ; Phenylalanine (47E5O17Y3R) ; Green Fluorescent Proteins (147336-22-9) ; DNA (9007-49-2) ; Chemokines
    Language English
    Publishing date 2023-10-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1024041-x
    ISSN 1520-4812 ; 1043-1802
    ISSN (online) 1520-4812
    ISSN 1043-1802
    DOI 10.1021/acs.bioconjchem.3c00390
    Database MEDical Literature Analysis and Retrieval System OnLINE

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