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    Area of Science:

    • Biochemistry
    • Chemical Biology
    • Proteomics

    Background:

    • Small molecule inhibitors often incompletely block protein functions.
    • Understanding the cellular consequences of partial inhibition is challenging.
    • Multifunctional proteins require tools to study inhibitor-bound states.

    Purpose of the Study:

    • To develop a chemoproteomic strategy for characterizing inhibitor-bound kinase localization and interactomes.
    • To investigate how inhibiting the multidomain kinase Src affects its cellular interactions.
    • To provide a method for studying druggable protein targets in complex cellular environments.

    Main Methods:

    • Utilized orthogonal inhibitors with a trans-cyclooctene (TCO) click handle.
    • Employed chemoproteomic enrichment and characterization of inhibitor-Src complexes.
    • Applied proximity ligation assays with TCO-conjugated probes for in situ studies.

    Main Results:

    • Src's cellular interactions are modulated by regulatory domain accessibility, influenced by its ATP-binding site.
    • Cellular signaling status significantly impacts Src's interactome.
    • TCO-probes enabled in situ studies of Src localization and interactions.

    Conclusions:

    • The developed chemoproteomic strategy comprehensively analyzes inhibitor-bound kinase localization and interactomes.
    • This method offers utility for studying multifunctional proteins and other druggable targets.
    • Allosteric modulation and cellular signaling are key factors in kinase interactions.