Deciphering the intimate relation of Huntingtin protein with the different cytoskeletons present in neurons (Actin and Microtubule) using expansion and high-resolution microscopy.
Abstract
Huntingtin is a scaffold protein in which an abnormal number of glutamine repetition leads to a neurodegenerative disease (Huntington’s disease). The normal Huntingtin protein possesses several properties that are related to its capacity to bind the cytoskeletons of actin and microtubule. Its capacity to recognize different structure of these cytoskeleton -e.g Actin periodic structure or microtubule composed of modified tubulin (acetylation, detyrosination)- has not been described yet because of the physical resolution-limit of light microscopy.
We propose to use expansion microscopy, a technic that increases the size of objects crosslinked into acrylamide gels, to interrogate the presence of Huntingtin in specific structure of the neuronal cytoskeletons.
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