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Narayan, K. B.

Publications and source records attributed to Narayan, K. B..

2 recordsLinked to original sources

Strategic Modulation of Polarity and Viscosity Sensitivity of Bimane Molecular Rotor-Based Fluorophores for Imaging α-Synuclein

Molecular rotor-based fluorophores (RBFs) that are target-selective and sensitive to both polarity and viscosity are valuable for diverse biological applications. Here, we have designed next-generation RBFs based on the underexplored bimane fluorophore through either changing in aryl substitution or varying {pi}-linkages between the rotatable electron donors and acceptors to produce red-shifted fluorescence emissions with large Stokes shifts. RBFs exhibit a twisted intramolecular charge transfer mechanism that enables control of polarity and viscosity sensitivity, as well as target selectivity. These features enable their application in: (1) turn-on fluorescent detection of -synuclein (S) fibrils, a hallmark of Parkinsons disease (PD), including amplified fibrils from patient samples; (2) monitoring early misfolding and oligomer formation during S aggregation; and (3) selective imaging of S condensates formed by liquid-liquid phase separation (LLPS). In all three cases, we show that our probes have high levels of selectivity for S versus other aggregating proteins. These properties enable one to study the interplay of S and tau in amyloid aggregation and the mechanisms underlying neurodegenerative disorders.

biochemistry↗

VASP phase separation with priming proteins of fast endophilin mediated endocytosis modulates actin polymerization

Actin polymerization is essential in several clathrin-independent endocytic pathways including fast endophilin mediated endocytosis (FEME), however the actin machinery involved in FEME has been elusive. Here, we show that the actin polymerase VASP colocalizes and interacts directly with the FEME priming complex. We identify Endophilin as a VASP binding partner and establish novel non-canonical interactions between Endophilin and VASP. The major FEME regulators Endophilin and Lamellipodin interact multivalently with VASP to form liquid-like condensates both in solution and on lipid membranes that localize actin polymerization with the extent of actin polymerized regulated by multivalent Endophilin-Lamellipodin interactions. We identify a novel function for Endophilin condensates in bundling actin filaments and show that Endophilin directly binds filamentous actin. Our findings support a model that explains the connection between local actin polymerization and dynamic formation and dissolution of endocytic priming patches in FEME.

biochemistry↗