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Lisbeth Schmidt Laursen

Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K

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Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K. / Laursen, Lisbeth Schmidt; Chan, Colin W; ffrench-Constant, Charles.

In: Journal of Cell Biology, Vol. 192, No. 5, 07.03.2011, p. 797-811.

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Laursen, Lisbeth Schmidt ; Chan, Colin W ; ffrench-Constant, Charles. / Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K. In: Journal of Cell Biology. 2011 ; Vol. 192, No. 5. pp. 797-811.

Bibtex

@article{c1c363cfd4c84fec914861b43125a074,
title = "Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K",
abstract = "Myelination in the central nervous system provides a unique example of how cells establish asymmetry. The myelinating cell, the oligodendrocyte, extends processes to and wraps multiple axons of different diameter, keeping the number of wraps proportional to the axon diameter. Local regulation of protein synthesis represents one mechanism used to control the different requirements for myelin sheath at each axo–glia interaction. Prior work has established that β1-integrins are involved in the axoglial interactions that initiate myelination. Here, we show that integrin activation regulates translation of a key sheath protein, myelin basic protein (MBP), by reversing the inhibitory effect of the mRNA 3′UTR. During oligodendrocyte differentiation and myelination α6β1-integrin interacts with hnRNP-K, an mRNA-binding protein, which binds to MBP mRNA and translocates from the nucleus to the myelin sheath. Furthermore, knockdown of hnRNP-K inhibits MBP protein synthesis during myelination. Together, these results identify a novel pathway by which axoglial adhesion molecules coordinate MBP synthesis with myelin sheath formation",
author = "Laursen, {Lisbeth Schmidt} and Chan, {Colin W} and Charles ffrench-Constant",
note = "MEDLINE{\textregistered} is the source for the MeSH terms of this document.",
year = "2011",
month = mar,
day = "7",
doi = "10.1083/jcb.201007014",
language = "English",
volume = "192",
pages = "797--811",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "5",

}

RIS

TY - JOUR

T1 - Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K

AU - Laursen, Lisbeth Schmidt

AU - Chan, Colin W

AU - ffrench-Constant, Charles

N1 - MEDLINE® is the source for the MeSH terms of this document.

PY - 2011/3/7

Y1 - 2011/3/7

N2 - Myelination in the central nervous system provides a unique example of how cells establish asymmetry. The myelinating cell, the oligodendrocyte, extends processes to and wraps multiple axons of different diameter, keeping the number of wraps proportional to the axon diameter. Local regulation of protein synthesis represents one mechanism used to control the different requirements for myelin sheath at each axo–glia interaction. Prior work has established that β1-integrins are involved in the axoglial interactions that initiate myelination. Here, we show that integrin activation regulates translation of a key sheath protein, myelin basic protein (MBP), by reversing the inhibitory effect of the mRNA 3′UTR. During oligodendrocyte differentiation and myelination α6β1-integrin interacts with hnRNP-K, an mRNA-binding protein, which binds to MBP mRNA and translocates from the nucleus to the myelin sheath. Furthermore, knockdown of hnRNP-K inhibits MBP protein synthesis during myelination. Together, these results identify a novel pathway by which axoglial adhesion molecules coordinate MBP synthesis with myelin sheath formation

AB - Myelination in the central nervous system provides a unique example of how cells establish asymmetry. The myelinating cell, the oligodendrocyte, extends processes to and wraps multiple axons of different diameter, keeping the number of wraps proportional to the axon diameter. Local regulation of protein synthesis represents one mechanism used to control the different requirements for myelin sheath at each axo–glia interaction. Prior work has established that β1-integrins are involved in the axoglial interactions that initiate myelination. Here, we show that integrin activation regulates translation of a key sheath protein, myelin basic protein (MBP), by reversing the inhibitory effect of the mRNA 3′UTR. During oligodendrocyte differentiation and myelination α6β1-integrin interacts with hnRNP-K, an mRNA-binding protein, which binds to MBP mRNA and translocates from the nucleus to the myelin sheath. Furthermore, knockdown of hnRNP-K inhibits MBP protein synthesis during myelination. Together, these results identify a novel pathway by which axoglial adhesion molecules coordinate MBP synthesis with myelin sheath formation

UR - http://www.scopus.com/inward/record.url?scp=79952412205&partnerID=8YFLogxK

U2 - 10.1083/jcb.201007014

DO - 10.1083/jcb.201007014

M3 - Journal article

C2 - 21357748

AN - SCOPUS:79952412205

VL - 192

SP - 797

EP - 811

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 5

ER -