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Regulation of PTP1B activation through disruption of redox-complex formation
We have identified a molecular interaction between the reversibly oxidized form of PTP1B and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B, prevented PTP1B inactivation by ROS and decreased EGFR phosphorylation. Our data suggest that destabi...
| Autores principales: | , , , , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
2019
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982540/ https://www.ncbi.nlm.nih.gov/pubmed/31873221 http://dx.doi.org/10.1038/s41589-019-0433-0 |
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| author | Londhe, Avinash D. Bergeron, Alexandre Curley, Stephanie M. Zhang, Fuming Rivera, Keith D. Kannan, Akaash Coulis, Gérald Rizvi, Syed H. M. Kim, Seung Jun Pappin, Darryl J. Tonks, Nicholas K. Linhardt, Robert J. Boivin, Benoit |
| author_facet | Londhe, Avinash D. Bergeron, Alexandre Curley, Stephanie M. Zhang, Fuming Rivera, Keith D. Kannan, Akaash Coulis, Gérald Rizvi, Syed H. M. Kim, Seung Jun Pappin, Darryl J. Tonks, Nicholas K. Linhardt, Robert J. Boivin, Benoit |
| author_sort | Londhe, Avinash D. |
| collection | PubMed |
| description | We have identified a molecular interaction between the reversibly oxidized form of PTP1B and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B, prevented PTP1B inactivation by ROS and decreased EGFR phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells. |
| format | Online Article Text |
| id | pubmed-6982540 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2019 |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-69825402020-06-23 Regulation of PTP1B activation through disruption of redox-complex formation Londhe, Avinash D. Bergeron, Alexandre Curley, Stephanie M. Zhang, Fuming Rivera, Keith D. Kannan, Akaash Coulis, Gérald Rizvi, Syed H. M. Kim, Seung Jun Pappin, Darryl J. Tonks, Nicholas K. Linhardt, Robert J. Boivin, Benoit Nat Chem Biol Article We have identified a molecular interaction between the reversibly oxidized form of PTP1B and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B, prevented PTP1B inactivation by ROS and decreased EGFR phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells. 2019-12-23 2020-02 /pmc/articles/PMC6982540/ /pubmed/31873221 http://dx.doi.org/10.1038/s41589-019-0433-0 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
| spellingShingle | Article Londhe, Avinash D. Bergeron, Alexandre Curley, Stephanie M. Zhang, Fuming Rivera, Keith D. Kannan, Akaash Coulis, Gérald Rizvi, Syed H. M. Kim, Seung Jun Pappin, Darryl J. Tonks, Nicholas K. Linhardt, Robert J. Boivin, Benoit Regulation of PTP1B activation through disruption of redox-complex formation |
| title | Regulation of PTP1B activation through disruption of redox-complex formation |
| title_full | Regulation of PTP1B activation through disruption of redox-complex formation |
| title_fullStr | Regulation of PTP1B activation through disruption of redox-complex formation |
| title_full_unstemmed | Regulation of PTP1B activation through disruption of redox-complex formation |
| title_short | Regulation of PTP1B activation through disruption of redox-complex formation |
| title_sort | regulation of ptp1b activation through disruption of redox-complex formation |
| topic | Article |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982540/ https://www.ncbi.nlm.nih.gov/pubmed/31873221 http://dx.doi.org/10.1038/s41589-019-0433-0 |
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