The membrane periodic skeleton is an actomyosin network that regulates axonal diameter and conduction

Autor: Inês Mendes Pinto, Diana Machado, David Rosa, Ana Costa, Ana Catarina Costa, Paula Sampaio, Marko Lampe, Feng Quan Zhou, Cátia D. F. Lopes, Paulo Aguiar, Rita Pinto-Costa, Luis Pajuelo, Xuewei Wang, Boris Rubinstein, Mónica Mendes Sousa, Sara C. Sousa, António J. Pereira, José C. Mateus
Přispěvatelé: Instituto de Investigação e Inovação em Saúde
Jazyk: angličtina
Rok vydání: 2020
Předmět:
0301 basic medicine
Contraction (grammar)
axonal cytoskeleton
Actomyosin / physiology
Neural Conduction
Hippocampal formation
Mice
0302 clinical medicine
Myosin
Spectrin
axonal diameter
Neural Conduction / physiology
Axon
Biology (General)
Nonmuscle Myosin Type IIB
Nonmuscle Myosin Type IIA
General Neuroscience
actin ring
Actomyosin
General Medicine
non-muscle myosin-ii
Axons / physiology
Nonmuscle Myosin Type IIA / metabolism
Nonmuscle Myosin Type IIB / metabolism
medicine.anatomical_structure
Membrane
Medicine
QH301-705.5
Science
Nonmuscle Myosin Type IIB / genetics
Short Report
macromolecular substances
General Biochemistry
Genetics and Molecular Biology

Cell Line
03 medical and health sciences
medicine
Animals
Humans
Actin
General Immunology and Microbiology
Nonmuscle Myosin Type IIA / genetics
Cell Biology
Axons
axonal electrophysiology
Rats
Electrophysiology
030104 developmental biology
nervous system
Biophysics
Rat
030217 neurology & neurosurgery
Neuroscience
Zdroj: eLife, Vol 9 (2020)
eLife
Popis: Neurons have a membrane periodic skeleton (MPS) composed of actin rings interconnected by spectrin. Here, combining chemical and genetic gain- and loss-of-function assays, we show that in rat hippocampal neurons the MPS is an actomyosin network that controls axonal expansion and contraction. Using super-resolution microscopy, we analyzed the localization of axonal non-muscle myosin II (NMII). We show that active NMII light chains are colocalized with actin rings and organized in a circular periodic manner throughout the axon shaft. In contrast, NMII heavy chains are mostly positioned along the longitudinal axonal axis, being able to crosslink adjacent rings. NMII filaments can play contractile or scaffolding roles determined by their position relative to actin rings and activation state. We also show that MPS destabilization through NMII inactivation affects axonal electrophysiology, increasing action potential conduction velocity. In summary, our findings open new perspectives on axon diameter regulation, with important implications in neuronal biology.
Databáze: OpenAIRE