beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones

<p>Abstract</p> <p>Several myelin-associated factors that inhibit axon growth of mature neurons, including Nogo66, myelin-associated glycoprotein (MAG) and oligodendrocyte myelin glycoprotein (OMgp), can associate with a common GPI-linked protein Nogo-66 receptor (NgR). Accumulatin...

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Main Authors: Goh Eyleen LK, Young Ju, Kuwako Kenichiro, Tessier-Lavigne Marc, He Zhigang, Griffin John W, Ming Guo-li
Format: Article
Language:English
Published: BMC 2008-10-01
Series:Molecular Brain
Online Access:http://www.molecularbrain.com/content/1/1/10
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spelling doaj-d72a81ad72d24ea2b1762493e1a699372020-11-24T21:54:54ZengBMCMolecular Brain1756-66062008-10-01111010.1186/1756-6606-1-10beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth conesGoh Eyleen LKYoung JuKuwako KenichiroTessier-Lavigne MarcHe ZhigangGriffin John WMing Guo-li<p>Abstract</p> <p>Several myelin-associated factors that inhibit axon growth of mature neurons, including Nogo66, myelin-associated glycoprotein (MAG) and oligodendrocyte myelin glycoprotein (OMgp), can associate with a common GPI-linked protein Nogo-66 receptor (NgR). Accumulating evidence suggests that myelin inhibitors also signal through unknown NgR-independent mechanisms. Here we show that MAG, a RGD tri-peptide containing protein, forms a complex with β1-integrin to mediate axonal growth cone turning responses of several neuronal types. Mutations that alter the RGD motif in MAG or inhibition of β1-integrin function, but not removal of NgRs, abolish these MAG-dependent events. In contrast, OMgp-induced repulsion is not affected by inhibition of b1-integrin function. We further show that MAG stimulates tyrosine phosphorylation of focal adhesion kinase (FAK), which in turn is required for MAG-induced growth cone turning. These studies identify β1-integrin as a specific mediator for MAG in growth cone turning responses, acting through FAK activation.</p> http://www.molecularbrain.com/content/1/1/10
collection DOAJ
language English
format Article
sources DOAJ
author Goh Eyleen LK
Young Ju
Kuwako Kenichiro
Tessier-Lavigne Marc
He Zhigang
Griffin John W
Ming Guo-li
spellingShingle Goh Eyleen LK
Young Ju
Kuwako Kenichiro
Tessier-Lavigne Marc
He Zhigang
Griffin John W
Ming Guo-li
beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
Molecular Brain
author_facet Goh Eyleen LK
Young Ju
Kuwako Kenichiro
Tessier-Lavigne Marc
He Zhigang
Griffin John W
Ming Guo-li
author_sort Goh Eyleen LK
title beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
title_short beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
title_full beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
title_fullStr beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
title_full_unstemmed beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
title_sort beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
publisher BMC
series Molecular Brain
issn 1756-6606
publishDate 2008-10-01
description <p>Abstract</p> <p>Several myelin-associated factors that inhibit axon growth of mature neurons, including Nogo66, myelin-associated glycoprotein (MAG) and oligodendrocyte myelin glycoprotein (OMgp), can associate with a common GPI-linked protein Nogo-66 receptor (NgR). Accumulating evidence suggests that myelin inhibitors also signal through unknown NgR-independent mechanisms. Here we show that MAG, a RGD tri-peptide containing protein, forms a complex with β1-integrin to mediate axonal growth cone turning responses of several neuronal types. Mutations that alter the RGD motif in MAG or inhibition of β1-integrin function, but not removal of NgRs, abolish these MAG-dependent events. In contrast, OMgp-induced repulsion is not affected by inhibition of b1-integrin function. We further show that MAG stimulates tyrosine phosphorylation of focal adhesion kinase (FAK), which in turn is required for MAG-induced growth cone turning. These studies identify β1-integrin as a specific mediator for MAG in growth cone turning responses, acting through FAK activation.</p>
url http://www.molecularbrain.com/content/1/1/10
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