The actin-spectrin submembrane scaffold restricts endocytosis along proximal axons

Author:

Wernert Florian1ORCID,Moparthi Satish Babu2,Pelletier Florence1ORCID,Lainé Jeanne3,Simons Eline1,Moulay Gilles2,Rueda Fanny1ORCID,Jullien Nicolas1ORCID,Benkhelifa-Ziyyat Sofia2,Papandréou Marie-Jeanne1ORCID,Leterrier Christophe1ORCID,Vassilopoulos Stéphane2ORCID

Affiliation:

1. Aix Marseille Université, CNRS, INP UMR7051, NeuroCyto, 13005 Marseille, France.

2. Sorbonne Université, INSERM, Institute of Myology, Centre of Research in Myology, UMRS 974, Paris, France.

3. Sorbonne Université, Department of Physiology, Faculty of Medicine Pitié-Salpêtrière, Paris, France.

Abstract

Clathrin-mediated endocytosis has characteristic features in neuronal dendrites and presynapses, but how membrane proteins are internalized along the axon shaft remains unclear. We focused on clathrin-coated structures and endocytosis along the axon initial segment (AIS) and their relationship to the periodic actin-spectrin scaffold that lines the axonal plasma membrane. A combination of super-resolution microscopy and platinum-replica electron microscopy on cultured neurons revealed that AIS clathrin-coated pits form within “clearings”, circular areas devoid of actin-spectrin mesh. Actin-spectrin scaffold disorganization increased clathrin-coated pit formation. Cargo uptake and live-cell imaging showed that AIS clathrin-coated pits are particularly stable. Neuronal plasticity-inducing stimulation triggered internalization of the clathrin-coated pits through polymerization of branched actin around them. Thus, spectrin and actin regulate clathrin-coated pit formation and scission to control endocytosis at the AIS.

Publisher

American Association for the Advancement of Science (AAAS)

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