Superresolution microscopy reveals distinct localisation of full length IRSp53 and its I-BAR domain protein within filopodia.

ABSTRACT: Superresolution microscopy offers the advantage of imaging biological structures within cells at the nano-scale. Here we apply two superresolution microscopy techniques, specifically 3D structured illumination microscopy (3D-SIM) and direct stochastic optical reconstruction microscopy (dSTORM), a type of single molecule localisation microscopy, to localise IRSp53 protein and its I-BAR domain in relation to F-actin within filopodia. IRSp53 generates dynamic (extending and retracting) filopodia 300 nm wide with a distinct gap between IRSp53 and F-actin. By contrast, protrusions induced by the I-BAR domain alone are non-dynamic measuring between 100-200 nm in width and exhibit a comparatively closer localisation of the I-BAR domain with the F-actin. The data suggest that IRSp53 membrane local

SUBMITTER: Sudhaharan T 

PROVIDER: S-EPMC6385187 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature