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Making myelin basic protein -from mRNA transport to localized translation

In the central nervous system (CNS) of most vertebrates, oligodendrocytes enwrap neuronal axons with extensions of their plasma membrane to form the myelin sheath. Several proteins are characteristically found in myelin of which myelin basic protein (MBP) is the second most abundant one after proteo...

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Autores principales: Müller, Christina, Bauer, Nina M., Schäfer, Isabelle, White, Robin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3784684/
https://www.ncbi.nlm.nih.gov/pubmed/24098271
http://dx.doi.org/10.3389/fncel.2013.00169
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author Müller, Christina
Bauer, Nina M.
Schäfer, Isabelle
White, Robin
author_facet Müller, Christina
Bauer, Nina M.
Schäfer, Isabelle
White, Robin
author_sort Müller, Christina
collection PubMed
description In the central nervous system (CNS) of most vertebrates, oligodendrocytes enwrap neuronal axons with extensions of their plasma membrane to form the myelin sheath. Several proteins are characteristically found in myelin of which myelin basic protein (MBP) is the second most abundant one after proteolipid protein. The lack of functional MBP in rodents results in a severe hypomyelinated phenotype in the CNS demonstrating its importance for myelin synthesis. Mbp mRNA is transported from the nucleus to the plasma membrane and is translated locally at the axon–glial contact site. Axonal properties such as diameter or electrical activity influence the degree of myelination. As oligodendrocytes can myelinate many axonal segments with varying properties, localized MBP translation represents an important part of a rapid and axon-tailored synthesis machinery. MBP’s ability to compact cellular membranes may be problematic for the integrity of intracellular membranous organelles and can also explain why MBP is transported in oligodendrocytes in the form of an mRNA rather than as a protein. Here we review the recent findings regarding intracellular transport and signaling mechanisms leading to localized translation of Mbp mRNA in oligodendrocytes. More detailed insights into the MBP synthesis pathway are important for a better understanding of the myelination process and may foster the development of remyelination therapies for demyelinating diseases.
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spelling pubmed-37846842013-10-04 Making myelin basic protein -from mRNA transport to localized translation Müller, Christina Bauer, Nina M. Schäfer, Isabelle White, Robin Front Cell Neurosci Neuroscience In the central nervous system (CNS) of most vertebrates, oligodendrocytes enwrap neuronal axons with extensions of their plasma membrane to form the myelin sheath. Several proteins are characteristically found in myelin of which myelin basic protein (MBP) is the second most abundant one after proteolipid protein. The lack of functional MBP in rodents results in a severe hypomyelinated phenotype in the CNS demonstrating its importance for myelin synthesis. Mbp mRNA is transported from the nucleus to the plasma membrane and is translated locally at the axon–glial contact site. Axonal properties such as diameter or electrical activity influence the degree of myelination. As oligodendrocytes can myelinate many axonal segments with varying properties, localized MBP translation represents an important part of a rapid and axon-tailored synthesis machinery. MBP’s ability to compact cellular membranes may be problematic for the integrity of intracellular membranous organelles and can also explain why MBP is transported in oligodendrocytes in the form of an mRNA rather than as a protein. Here we review the recent findings regarding intracellular transport and signaling mechanisms leading to localized translation of Mbp mRNA in oligodendrocytes. More detailed insights into the MBP synthesis pathway are important for a better understanding of the myelination process and may foster the development of remyelination therapies for demyelinating diseases. Frontiers Media S.A. 2013-09-27 /pmc/articles/PMC3784684/ /pubmed/24098271 http://dx.doi.org/10.3389/fncel.2013.00169 Text en Copyright © Müller, Bauer, Schäfer and White. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Müller, Christina
Bauer, Nina M.
Schäfer, Isabelle
White, Robin
Making myelin basic protein -from mRNA transport to localized translation
title Making myelin basic protein -from mRNA transport to localized translation
title_full Making myelin basic protein -from mRNA transport to localized translation
title_fullStr Making myelin basic protein -from mRNA transport to localized translation
title_full_unstemmed Making myelin basic protein -from mRNA transport to localized translation
title_short Making myelin basic protein -from mRNA transport to localized translation
title_sort making myelin basic protein -from mrna transport to localized translation
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3784684/
https://www.ncbi.nlm.nih.gov/pubmed/24098271
http://dx.doi.org/10.3389/fncel.2013.00169
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