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Temporal Profiling Establishes a Dynamic S-Palmitoylation Cycle.

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    Dynamic S-palmitoylation, crucial for protein function, was studied using a new bioorthogonal assay. Inhibiting depalmitoylase enzymes increased labeling but didn't alter overall protein S-palmitoylation levels.

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    Area of Science:

    • Biochemistry
    • Proteomics
    • Cell Biology

    Background:

    • S-palmitoylation is vital for membrane protein localization, trafficking, and function.
    • Previous studies hinted at dynamic S-palmitoylation regulated by enzymes, but its full scope was unknown.

    Purpose of the Study:

    • To develop and utilize a pulsed bioorthogonal S-palmitoylation assay for temporal analysis.
    • To investigate the impact of depalmitoylase inhibition on S-palmitoylation dynamics.

    Main Methods:

    • Developed a pulsed bioorthogonal S-palmitoylation assay using hexadecylfluorophosphonate (HDFP).
    • Inhibited APT and ABHD17 depalmitoylase families with HDFP to analyze S-palmitoylation kinetics.
    • Performed S-palmitoylation profiling in APT1/2 knockout mouse brains.

    Main Results:

    • HDFP treatment increased alkynyl-fatty acid labeling and revealed kinetically distinct S-palmitoylated protein subgroups.
    • Surprisingly, HDFP did not alter steady-state S-palmitoylation levels despite depalmitoylase inhibition.
    • S-palmitoylation profiling in knockout brains also showed no change in overall S-palmitoylation levels.
    • Compared to other methods, bioorthogonal labeling identified a smaller fraction of dynamic proteins, suggesting greater S-palmitoylation stability.

    Conclusions:

    • Disrupting depalmitoylase activity enhances labeling of dynamic S-palmitoylated proteins but does not significantly change proteome-wide steady-state levels.
    • The findings suggest S-palmitoylation may be more stable than previously assumed.
    • The developed assay provides a tool for temporal analysis of S-palmitoylation dynamics.