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Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein
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Zeitschriftentitel: | The Journal of Neuroscience |
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Personen und Körperschaften: | , , , , , , , |
In: | The Journal of Neuroscience, 29, 2009, 5, S. 1480-1485 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Society for Neuroscience
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Schlagwörter: |
author_facet |
Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing |
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author |
Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing |
spellingShingle |
Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing The Journal of Neuroscience Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein General Neuroscience |
author_sort |
liu, jun |
spelling |
Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.6202-08.2009 <jats:p>Growing evidence suggests that extracellular α-synuclein (eSNCA) may play an important role in the pathogenesis of Parkinson's disease (PD) and related synucleinopathies by producing neurotoxicity directly or via activation of glia. However, the mechanisms involved in the trafficking of eSNCA in neurons and/or glia remain unclear. Here, we demonstrated that eSNCA could be resecreted out of neurons via a process modulated by a recycling endosome regulator rab11a in addition to being degraded by an endosome–lysosome system. A quantitative proteomic analysis also revealed numerous proteins through which rab11a might execute its function. One of the candidate proteins, heat shock protein 90 (HSP90), was validated to be interacting with rab11a. Furthermore, geldanamycin, an HSP90 inhibitor, not only prevented resecretion of eSNCA but also attenuated neurotoxicity induced by eSNCA.</jats:p> Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein The Journal of Neuroscience |
doi_str_mv |
10.1523/jneurosci.6202-08.2009 |
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Society for Neuroscience, 2009 |
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Society for Neuroscience |
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The Journal of Neuroscience |
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title |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_unstemmed |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_full |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_fullStr |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_full_unstemmed |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_short |
Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_sort |
rab11a and hsp90 regulate recycling of extracellular α-synuclein |
topic |
General Neuroscience |
url |
http://dx.doi.org/10.1523/jneurosci.6202-08.2009 |
publishDate |
2009 |
physical |
1480-1485 |
description |
<jats:p>Growing evidence suggests that extracellular α-synuclein (eSNCA) may play an important role in the pathogenesis of Parkinson's disease (PD) and related synucleinopathies by producing neurotoxicity directly or via activation of glia. However, the mechanisms involved in the trafficking of eSNCA in neurons and/or glia remain unclear. Here, we demonstrated that eSNCA could be resecreted out of neurons via a process modulated by a recycling endosome regulator rab11a in addition to being degraded by an endosome–lysosome system. A quantitative proteomic analysis also revealed numerous proteins through which rab11a might execute its function. One of the candidate proteins, heat shock protein 90 (HSP90), was validated to be interacting with rab11a. Furthermore, geldanamycin, an HSP90 inhibitor, not only prevented resecretion of eSNCA but also attenuated neurotoxicity induced by eSNCA.</jats:p> |
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author | Liu, Jun, Zhang, Jian-Peng, Shi, Min, Quinn, Thomas, Bradner, Joshua, Beyer, Richard, Chen, Shengdi, Zhang, Jing |
author_facet | Liu, Jun, Zhang, Jian-Peng, Shi, Min, Quinn, Thomas, Bradner, Joshua, Beyer, Richard, Chen, Shengdi, Zhang, Jing, Liu, Jun, Zhang, Jian-Peng, Shi, Min, Quinn, Thomas, Bradner, Joshua, Beyer, Richard, Chen, Shengdi, Zhang, Jing |
author_sort | liu, jun |
container_issue | 5 |
container_start_page | 1480 |
container_title | The Journal of Neuroscience |
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description | <jats:p>Growing evidence suggests that extracellular α-synuclein (eSNCA) may play an important role in the pathogenesis of Parkinson's disease (PD) and related synucleinopathies by producing neurotoxicity directly or via activation of glia. However, the mechanisms involved in the trafficking of eSNCA in neurons and/or glia remain unclear. Here, we demonstrated that eSNCA could be resecreted out of neurons via a process modulated by a recycling endosome regulator rab11a in addition to being degraded by an endosome–lysosome system. A quantitative proteomic analysis also revealed numerous proteins through which rab11a might execute its function. One of the candidate proteins, heat shock protein 90 (HSP90), was validated to be interacting with rab11a. Furthermore, geldanamycin, an HSP90 inhibitor, not only prevented resecretion of eSNCA but also attenuated neurotoxicity induced by eSNCA.</jats:p> |
doi_str_mv | 10.1523/jneurosci.6202-08.2009 |
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source_id | 49 |
spelling | Liu, Jun Zhang, Jian-Peng Shi, Min Quinn, Thomas Bradner, Joshua Beyer, Richard Chen, Shengdi Zhang, Jing 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.6202-08.2009 <jats:p>Growing evidence suggests that extracellular α-synuclein (eSNCA) may play an important role in the pathogenesis of Parkinson's disease (PD) and related synucleinopathies by producing neurotoxicity directly or via activation of glia. However, the mechanisms involved in the trafficking of eSNCA in neurons and/or glia remain unclear. Here, we demonstrated that eSNCA could be resecreted out of neurons via a process modulated by a recycling endosome regulator rab11a in addition to being degraded by an endosome–lysosome system. A quantitative proteomic analysis also revealed numerous proteins through which rab11a might execute its function. One of the candidate proteins, heat shock protein 90 (HSP90), was validated to be interacting with rab11a. Furthermore, geldanamycin, an HSP90 inhibitor, not only prevented resecretion of eSNCA but also attenuated neurotoxicity induced by eSNCA.</jats:p> Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein The Journal of Neuroscience |
spellingShingle | Liu, Jun, Zhang, Jian-Peng, Shi, Min, Quinn, Thomas, Bradner, Joshua, Beyer, Richard, Chen, Shengdi, Zhang, Jing, The Journal of Neuroscience, Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein, General Neuroscience |
title | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_full | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_fullStr | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_full_unstemmed | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_short | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
title_sort | rab11a and hsp90 regulate recycling of extracellular α-synuclein |
title_unstemmed | Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein |
topic | General Neuroscience |
url | http://dx.doi.org/10.1523/jneurosci.6202-08.2009 |