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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....
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2010
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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. |
format | Text |
id | pubmed-2854096 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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