PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain
<p>Mouse protein tyrosine phosphatase PTPBR7 is a receptor-like, transmembrane protein that is localized on the surface of neuronal cells. Its protein phosphatase activity is reduced upon multimerization, and PTPBR7-deficient mice display motor coordination defects. Extracellular molecules tha...
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doaj-356eb848726a48c194d776ee30ba466e2020-11-24T23:46:37ZengIvyspring International PublisherInternational Journal of Biological Sciences1449-22882011-01-0177978991PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse BrainIrene M. Chesini, Griet Debyser, Huib Croes, Gerdy B. ten Dam, Bart Devreese, Andrew W. Stoker, Wiljan J.A.J. Hendriks<p>Mouse protein tyrosine phosphatase PTPBR7 is a receptor-like, transmembrane protein that is localized on the surface of neuronal cells. Its protein phosphatase activity is reduced upon multimerization, and PTPBR7-deficient mice display motor coordination defects. Extracellular molecules that may influence PTPBR7 activity, however, remain to be determined. We here show that the PTPBR7 extracellular domain binds to highly myelinated regions in mouse brain, in particular the white matter tracks in cerebellum. PTPBR7 deficiency does not alter this binding pattern, as witnessed by RAP in situ staining of <i>Ptprr</i><sup>-/-</sup> mouse brain sections. Additional <i>in situ</i> and <i>in vitro</i> experiments also suggest that sugar moieties of heparan sulphate and chondroitin sulphate glycosaminoglycans are not critical for PTPBR7 binding. Candidate binding proteins were affinity-purified exploiting the PTPBR7 extracellular domain and identified by mass spectrometric means. Results support the suggested link between PTPRR isoforms and cerebellar calcium ion homeostasis, and suggest an additional role in the process of cell-cell adhesion.</p>http://www.biolsci.org/v07p0978.htm |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Irene M. Chesini, Griet Debyser, Huib Croes, Gerdy B. ten Dam, Bart Devreese, Andrew W. Stoker, Wiljan J.A.J. Hendriks |
spellingShingle |
Irene M. Chesini, Griet Debyser, Huib Croes, Gerdy B. ten Dam, Bart Devreese, Andrew W. Stoker, Wiljan J.A.J. Hendriks PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain International Journal of Biological Sciences |
author_facet |
Irene M. Chesini, Griet Debyser, Huib Croes, Gerdy B. ten Dam, Bart Devreese, Andrew W. Stoker, Wiljan J.A.J. Hendriks |
author_sort |
Irene M. Chesini, Griet Debyser, Huib Croes, Gerdy B. ten Dam, Bart Devreese, Andrew W. Stoker, Wiljan J.A.J. Hendriks |
title |
PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain |
title_short |
PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain |
title_full |
PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain |
title_fullStr |
PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain |
title_full_unstemmed |
PTPBR7 Binding Proteins in Myelinating Neurons of the Mouse Brain |
title_sort |
ptpbr7 binding proteins in myelinating neurons of the mouse brain |
publisher |
Ivyspring International Publisher |
series |
International Journal of Biological Sciences |
issn |
1449-2288 |
publishDate |
2011-01-01 |
description |
<p>Mouse protein tyrosine phosphatase PTPBR7 is a receptor-like, transmembrane protein that is localized on the surface of neuronal cells. Its protein phosphatase activity is reduced upon multimerization, and PTPBR7-deficient mice display motor coordination defects. Extracellular molecules that may influence PTPBR7 activity, however, remain to be determined. We here show that the PTPBR7 extracellular domain binds to highly myelinated regions in mouse brain, in particular the white matter tracks in cerebellum. PTPBR7 deficiency does not alter this binding pattern, as witnessed by RAP in situ staining of <i>Ptprr</i><sup>-/-</sup> mouse brain sections. Additional <i>in situ</i> and <i>in vitro</i> experiments also suggest that sugar moieties of heparan sulphate and chondroitin sulphate glycosaminoglycans are not critical for PTPBR7 binding. Candidate binding proteins were affinity-purified exploiting the PTPBR7 extracellular domain and identified by mass spectrometric means. Results support the suggested link between PTPRR isoforms and cerebellar calcium ion homeostasis, and suggest an additional role in the process of cell-cell adhesion.</p> |
url |
http://www.biolsci.org/v07p0978.htm |
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