Biophysical Society Thematic Meeting | Tutzing 2026

Single-Molecule FRET: The Next 30 Years

Tuesday Speaker Abstracts

PHOSPHOREGULATION OF TAU FUNCTION Elizabeth Rhoades 1,2 ; Christopher R Brue 1,2 ; Yujing Fan 1 ; Sarah A Schick 1 ; Polina Holubovska 1 ; 1 University of Pennsylvania, Chemistry, Philadelphia, PA, USA 2 University of Pennsylvania Perelman School of Medicine, Biochemistry & Biophysics, Philadelphia, PA, USA The intrinsically disordered protein Tau plays an important role in modulating the dynamics and stability of axonal microtubules in neurons. Tubulin binding sites are found in Tau's proline-rich region (PRR), microtubule binding repeats (MTBRs), and pseudo-repeat (R'). Tau phosphorylation sites, which cluster with high frequency within the PRR, differentially regulate tubulin interactions although the molecular details are poorly. Here, we use single molecule Förster resonance energy transfer to probe the impact of phosphorylation on long range intramolecular interactions within Tau. We correlate these with tubulin binding and polymerization capacity to provide mechanistic insight into regulation of Tau function.

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