Immunoproximity biotinylation reveals the axon initial segment proteome

Wei Zhang, Yu Fu, Luxin Peng, Yuki Ogawa, Xiaoyun Ding, Anne Rasband, Xinyue Zhou, Maya Shelly, Matthew N. Rasband () and Peng Zou ()
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Wei Zhang: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University
Yu Fu: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University
Luxin Peng: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University
Yuki Ogawa: Baylor College of Medicine
Xiaoyun Ding: Baylor College of Medicine
Anne Rasband: Baylor College of Medicine
Xinyue Zhou: PKU-Tsinghua Center for Life Science, Peking University
Maya Shelly: Stony Brook University
Matthew N. Rasband: Baylor College of Medicine
Peng Zou: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-44015-2

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