Language
English
Publication Date
12-11-2023
Journal
Nature Communications
DOI
10.1038/s41467-023-44015-2
PMID
38081810
PMCID
PMC10713531
PubMedCentral® Posted Date
12-11-2023
PubMedCentral® Full Text Version
Post-print
Abstract
The axon initial segment (AIS) is a specialized neuronal compartment required for action potential generation and neuronal polarity. However, understanding the mechanisms regulating AIS structure and function has been hindered by an incomplete knowledge of its molecular composition. Here, using immuno-proximity biotinylation we further define the AIS proteome and its dynamic changes during neuronal maturation. Among the many AIS proteins identified, we show that SCRIB is highly enriched in the AIS both in vitro and in vivo, and exhibits a periodic architecture like the axonal spectrin-based cytoskeleton. We find that ankyrinG interacts with and recruits SCRIB to the AIS. However, loss of SCRIB has no effect on ankyrinG. This powerful and flexible approach further defines the AIS proteome and provides a rich resource to elucidate the mechanisms regulating AIS structure and function.
Keywords
Axon Initial Segment, Proteome, Biotinylation, Axons, Neurons, Molecular neuroscience, Cellular neuroscience, Proteomics, Proteomics
Published Open-Access
yes
Recommended Citation
Zhang, Wei; Fu, Yu; Peng, Luxin; et al., "Immunoproximity Biotinylation Reveals the Axon Initial Segment Proteome" (2023). Faculty, Staff and Students Publications. 7279.
https://digitalcommons.library.tmc.edu/baylor_docs/7279