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The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface

PTP1B bound to mature N-cadherin promotes the association of β-catenin into the complex, the stable expression of the complex at cell surface, and cadherin-mediated adhesion. Here we show that PTP1B is also required for N-cadherin precursor trafficking through early stages of the secretory pathway....

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Detalles Bibliográficos
Autores principales: Hernández, Mariana V., Wehrendt, Diana P., Arregui, Carlos O.
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854096/
https://www.ncbi.nlm.nih.gov/pubmed/20181825
http://dx.doi.org/10.1091/mbc.E09-10-0880
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author Hernández, Mariana V.
Wehrendt, Diana P.
Arregui, Carlos O.
author_facet Hernández, Mariana V.
Wehrendt, Diana P.
Arregui, Carlos O.
author_sort Hernández, Mariana V.
collection PubMed
description PTP1B bound to mature N-cadherin promotes the association of β-catenin into the complex, the stable expression of the complex at cell surface, and cadherin-mediated adhesion. Here we show that PTP1B is also required for N-cadherin precursor trafficking through early stages of the secretory pathway. This function does not require association of PTP1B with the precursor. In PTP1B null cells, the N-cadherin precursor showed higher sensitivity to endoglycosidase H than in cells reconstituted with the wild-type enzyme. It also showed slower kinetics of ER-to-Golgi translocation and processing. Trafficking of the viral stomatitis vesicular glycoprotein, VSV-G, however, revealed no differences between PTP1B null and reconstituted cells. N-cadherin precursor complexes contained similar levels of α- and β-catenin regardless of PTP1B expression. In contrast, the associated p120 catenin (p120) was significantly reduced in absence of PTP1B expression. An N-cadherin precursor construct defective in p120 binding, and expressed in PTP1B reconstituted cells, showed higher sensitivity to endoglycosidase H and slower kinetics of processing than the wild-type precursor. Our results suggest that PTP1B promotes the association of p120 to the N-cadherin precursor, facilitating the trafficking of the complex from the ER to the Golgi complex.
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spelling pubmed-28540962010-06-30 The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface Hernández, Mariana V. Wehrendt, Diana P. Arregui, Carlos O. Mol Biol Cell Articles PTP1B bound to mature N-cadherin promotes the association of β-catenin into the complex, the stable expression of the complex at cell surface, and cadherin-mediated adhesion. Here we show that PTP1B is also required for N-cadherin precursor trafficking through early stages of the secretory pathway. This function does not require association of PTP1B with the precursor. In PTP1B null cells, the N-cadherin precursor showed higher sensitivity to endoglycosidase H than in cells reconstituted with the wild-type enzyme. It also showed slower kinetics of ER-to-Golgi translocation and processing. Trafficking of the viral stomatitis vesicular glycoprotein, VSV-G, however, revealed no differences between PTP1B null and reconstituted cells. N-cadherin precursor complexes contained similar levels of α- and β-catenin regardless of PTP1B expression. In contrast, the associated p120 catenin (p120) was significantly reduced in absence of PTP1B expression. An N-cadherin precursor construct defective in p120 binding, and expressed in PTP1B reconstituted cells, showed higher sensitivity to endoglycosidase H and slower kinetics of processing than the wild-type precursor. Our results suggest that PTP1B promotes the association of p120 to the N-cadherin precursor, facilitating the trafficking of the complex from the ER to the Golgi complex. The American Society for Cell Biology 2010-04-15 /pmc/articles/PMC2854096/ /pubmed/20181825 http://dx.doi.org/10.1091/mbc.E09-10-0880 Text en © 2010 by The American Society for Cell Biology
spellingShingle Articles
Hernández, Mariana V.
Wehrendt, Diana P.
Arregui, Carlos O.
The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title_full The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title_fullStr The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title_full_unstemmed The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title_short The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface
title_sort protein tyrosine phosphatase ptp1b is required for efficient delivery of n-cadherin to the cell surface
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854096/
https://www.ncbi.nlm.nih.gov/pubmed/20181825
http://dx.doi.org/10.1091/mbc.E09-10-0880
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