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IDPs & Secretory Dysfunction (Aggregation–Secretion Axis)

IDPs & Secretory Dysfunction

Intrinsically disordered and amyloid‑prone proteins (α‑syn, Aβ, IAPP) can phase‑separate and aggregate, rewiring membrane trafficking and exocytosis by sequestering SNARE regulators, crowding release sites, altering PIP2/DAG, and diverting cargo to EVs.

Using minimal reconstitutions with native‑like asymmetric bilayers, we quantify how condensate‑proximal lipids and fusion clamps (synaptotagmin/complexin) set priming and Ca²⁺ thresholds.

We examine aggregate stress in neurons and β‑cells to link synaptic failure and loss of biphasic insulin secretion to IDP‑driven changes in vesicle pools.

Selected publications

  • Synergistic roles of synaptotagmin‑1 and complexin in exocytosis. eLife, 2020. See publications →
  • Synaptotagmin oligomers form a Ca²⁺‑sensitive fusion clamp. FEBS Letters, 2019. See publications →
  • Complete reconstitution reveals lipid control of priming/release. PNAS, 2023. See publications →