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Filopodial protrusion driven by density-dependent Ena-TOCA-1 interactions.

Thomas C A Blake1,2, Helen M Fox1,2, Vasja Urbančič1,2

  • 1Wellcome/Cancer Research UK Gurdon Institute, University of Cambridge, Cambridge CB2 1QN, UK.

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|February 7, 2024
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The neuronal adaptor protein TOCA-1 promotes filopodial protrusion by recruiting Ena/VASP proteins, independent of membrane curvature. This finding clarifies TOCA-1

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Cytoskeleton Dynamics

Background:

  • Filopodia are crucial actin-rich cellular protrusions in neuronal development.
  • Membrane-binding adaptor proteins regulate filopodia by linking membrane interactions to actin regulators.
  • F-BAR domain proteins, like TOCA-1, are key upstream regulators in these networks.

Purpose of the Study:

  • To investigate the role of the F-BAR domain protein TOCA-1 (FNBP1L) in filopodial dynamics.
  • To analyze the relationship between TOCA-1, Ena/VASP proteins, and filopodial protrusion in Xenopus retinal ganglion cells.

Main Methods:

  • Quantitative analysis of TOCA-1 and filopodial dynamics in vivo.
  • In vitro assessment of TOCA-1 density effects on Ena/VASP protein binding.
  • Two-colour single-molecule localization microscopy (SMLM) to study TOCA-1 and Ena nanoscale association.
  • Perturbation of Cdc42 activation using the small-molecule inhibitor CASIN.

Main Results:

  • Increased TOCA-1 density enhances Ena/VASP protein binding in vitro.
  • TOCA-1 accumulation and co-localization with Ena correlate with filopodial protrusion in vivo.
  • TOCA-1 clusters, dependent on a functional SH3 domain and Cdc42 activation, promote filopodial protrusion.
  • TOCA-1 and Ena exhibit nanoscale association.

Conclusions:

  • TOCA-1 clusters function independently of membrane curvature to recruit and promote Ena activity.
  • TOCA-1 plays a significant role in regulating filopodial protrusion via Ena/VASP recruitment.
  • Cdc42 activation is essential for TOCA-1-mediated filopodial extension.