Ionic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
26 03 2019
Historique:
received: 01 02 2019
accepted: 05 02 2019
pubmed: 14 2 2019
medline: 18 12 2019
entrez: 14 2 2019
Statut: ppublish

Résumé

The formation of a mature myelin sheath in the vertebrate nervous system requires specific protein-membrane interactions. Several myelin-specific proteins are involved in stacking lipid membranes into multilayered structures around axons, and misregulation of these processes may contribute to chronic demyelinating diseases. Two key proteins in myelin membrane binding and stacking are the myelin basic protein (MBP) and protein zero (P0). Other factors, including Ca

Identifiants

pubmed: 30755303
pii: S0006-291X(19)30212-8
doi: 10.1016/j.bbrc.2019.02.025
pii:
doi:

Substances chimiques

Membrane Lipids 0
Myelin Basic Protein 0
Myelin P0 Protein 0
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7-12

Informations de copyright

Copyright © 2019 Elsevier Inc. All rights reserved.

Auteurs

Arne Raasakka (A)

Department of Biomedicine, University of Bergen, Bergen, Norway.

Nykola C Jones (NC)

ISA, Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.

Søren Vrønning Hoffmann (SV)

ISA, Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.

Petri Kursula (P)

Department of Biomedicine, University of Bergen, Bergen, Norway; Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland. Electronic address: petri.kursula@uib.no.

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Classifications MeSH