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Paralemmin-1 controls the nanoarchitecture of the neuronal submembrane cytoskeleton

The submembrane cytoskeleton of neurons displays a highly ordered 190-nanometer periodic actin-spectrin lattice, the membrane-associated periodic skeleton (MPS). It is involved in mechanical resilience, signaling, and action potential transmission. Here, we identify paralemmin-1 (Palm1) as a compone...

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Hauptverfasser: Macarrón Palacios, Victor (VerfasserIn) , Hubrich, Jasmine (VerfasserIn) , do Rego Barros Fernandes Lima, Maria Augusta (VerfasserIn) , Metzendorf, Nicole (VerfasserIn) , Kneilmann, Simon (VerfasserIn) , Trapp, Marleen (VerfasserIn) , Acuna Goycolea, Claudio (VerfasserIn) , Patrizi, Annarita (VerfasserIn) , D’Este, Elisa (VerfasserIn) , Kilimann, Manfred (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 7 Mar 2025
In: Science advances
Year: 2025, Jahrgang: 11, Heft: 10, Pages: 1-21
ISSN:2375-2548
DOI:10.1126/sciadv.adt3724
Online-Zugang:Verlag, kostenfrei, Volltext: https://doi.org/10.1126/sciadv.adt3724
Verlag, kostenfrei, Volltext: https://www.science.org/doi/10.1126/sciadv.adt3724
Volltext
Verfasserangaben:Victor Macarrón-Palacios, Jasmine Hubrich, Maria Augusta do Rego Barros Fernandes Lima, Nicole G. Metzendorf, Simon Kneilmann, Marleen Trapp, Claudio Acuna, Annarita Patrizi, Elisa D’Este, Manfred W. Kilimann
Beschreibung
Zusammenfassung:The submembrane cytoskeleton of neurons displays a highly ordered 190-nanometer periodic actin-spectrin lattice, the membrane-associated periodic skeleton (MPS). It is involved in mechanical resilience, signaling, and action potential transmission. Here, we identify paralemmin-1 (Palm1) as a component and regulator of the MPS. Palm1 binds to the amino-terminal region of βII-spectrin, and MINFLUX microscopy localizes it in close proximity (<20 nanometers) to the actin-capping protein and MPS component adducin. Combining overexpression, knockout, and rescue experiments, we observe that the expression level of Palm1 controls the degree of periodicity of the MPS and also affects the electrophysiological properties of neurons. A single amino acid mutation (W54A) in Palm1 abolishes the MPS binding and remodeling activities of Palm1. Our findings identify Palm1 as a protein specifically dedicated to organizing the MPS and will advance the understanding of the assembly and plasticity of the actin-spectrin submembrane skeleton in general.
Beschreibung:Gesehen am 01.09.2025
Beschreibung:Online Resource
ISSN:2375-2548
DOI:10.1126/sciadv.adt3724

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