The axon initial segment (AIS), located within the first 30 $\mu$m of the axon, has two essential roles in generating action potentials and maintaining axonal identity. AIS assembly depends on a ßIV-spectrin/ankyrin G scaffold, but its macromolecular arrangement is not well understood. Here, we quantitatively determined the AIS nanoscale architecture by using stochastic optical reconstruction microscopy (STORM). First, we directly demonstrate that the 190-nm periodicity of the AIS submembrane lattice results from longitudinal, head-to-head ßIV-spectrin molecules connecting actin rings. Using multicolor 3D-STORM, we resolve the nanoscale organization of ankyrin G: its amino terminus associates with the submembrane lattice, whereas the C terminus radially extends (∼32 nm on average) toward the cytosol. This AIS nano-architecture is highly resistant to cytoskeletal perturbations, indicating its role in structural stabilization. Our findings provide a comprehensive view of AIS molecular architecture and will help reveal the crucial physiological functions of this compartment.
:C$\backslash$:/Users/Karoline/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Leterrier et al. - 2015 - Nanoscale Architecture of the Axon Initial Segment Reveals an Organized and Robust Scaffold.pdf:pdf
%0 Journal Article
%1 Leterrier2015
%A Leterrier, Christophe
%A Potier, Jean
%A Caillol, Ghislaine
%A Debarnot, Claire
%A Rueda Boroni, Fanny
%A Dargent, Bénédicte
%D 2015
%I Cell Press
%J Cell Reports
%K AIS axon cytoskeleton neuro team
%N 12
%P 2781--2793
%R 10.1016/J.CELREP.2015.11.051
%T Nanoscale Architecture of the Axon Initial Segment Reveals an Organized and Robust Scaffold
%U https://www.sciencedirect.com/science/article/pii/S2211124715013820
%V 13
%X The axon initial segment (AIS), located within the first 30 $\mu$m of the axon, has two essential roles in generating action potentials and maintaining axonal identity. AIS assembly depends on a ßIV-spectrin/ankyrin G scaffold, but its macromolecular arrangement is not well understood. Here, we quantitatively determined the AIS nanoscale architecture by using stochastic optical reconstruction microscopy (STORM). First, we directly demonstrate that the 190-nm periodicity of the AIS submembrane lattice results from longitudinal, head-to-head ßIV-spectrin molecules connecting actin rings. Using multicolor 3D-STORM, we resolve the nanoscale organization of ankyrin G: its amino terminus associates with the submembrane lattice, whereas the C terminus radially extends (∼32 nm on average) toward the cytosol. This AIS nano-architecture is highly resistant to cytoskeletal perturbations, indicating its role in structural stabilization. Our findings provide a comprehensive view of AIS molecular architecture and will help reveal the crucial physiological functions of this compartment.
@article{Leterrier2015,
abstract = {The axon initial segment (AIS), located within the first 30 $\mu$m of the axon, has two essential roles in generating action potentials and maintaining axonal identity. AIS assembly depends on a {\ss}IV-spectrin/ankyrin G scaffold, but its macromolecular arrangement is not well understood. Here, we quantitatively determined the AIS nanoscale architecture by using stochastic optical reconstruction microscopy (STORM). First, we directly demonstrate that the 190-nm periodicity of the AIS submembrane lattice results from longitudinal, head-to-head {\ss}IV-spectrin molecules connecting actin rings. Using multicolor 3D-STORM, we resolve the nanoscale organization of ankyrin G: its amino terminus associates with the submembrane lattice, whereas the C terminus radially extends (∼32 nm on average) toward the cytosol. This AIS nano-architecture is highly resistant to cytoskeletal perturbations, indicating its role in structural stabilization. Our findings provide a comprehensive view of AIS molecular architecture and will help reveal the crucial physiological functions of this compartment.},
added-at = {2020-03-23T21:12:34.000+0100},
author = {Leterrier, Christophe and Potier, Jean and Caillol, Ghislaine and Debarnot, Claire and {Rueda Boroni}, Fanny and Dargent, B{\'{e}}n{\'{e}}dicte},
biburl = {https://www.bibsonomy.org/bibtex/2e2bfef491f477d50e43c4c6f97448d63/kfriedl},
doi = {10.1016/J.CELREP.2015.11.051},
file = {:C$\backslash$:/Users/Karoline/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Leterrier et al. - 2015 - Nanoscale Architecture of the Axon Initial Segment Reveals an Organized and Robust Scaffold.pdf:pdf},
interhash = {a8c1897954d9daf6fd0a0d436e7cc250},
intrahash = {e2bfef491f477d50e43c4c6f97448d63},
issn = {2211-1247},
journal = {Cell Reports},
keywords = {AIS axon cytoskeleton neuro team},
month = dec,
number = 12,
pages = {2781--2793},
publisher = {Cell Press},
timestamp = {2020-04-07T10:43:11.000+0200},
title = {{Nanoscale Architecture of the Axon Initial Segment Reveals an Organized and Robust Scaffold}},
url = {https://www.sciencedirect.com/science/article/pii/S2211124715013820},
volume = 13,
year = 2015
}