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HMGB1 Mediates Autophagy Dysfunction via Perturbing Beclin1-Vps34 Complex in Dopaminergic Cell Model.

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Title: HMGB1 Mediates Autophagy Dysfunction via Perturbing Beclin1-Vps34 Complex in Dopaminergic Cell Model.
Authors: Jinsha Huang, Jiaolong Yang, Yan Shen, Haiyang Jiang, Chao Han, Guoxin Zhang, Ling Liu, Xiaoyun Xu, Jie Li, Zhicheng Lin, Nian Xiong, Zhentao Zhang, Jing Xiong, Tao Wang, Carri, Maria Teresa, Hong Qing
Source: Frontiers in Molecular Neuroscience; 1/31/2017, Vol. 10, p1-11, 11p
Subject Terms: HIGH mobility group proteins, DOPAMINERGIC mechanisms, PARKINSON'S disease
Abstract: Parkinson's disease (PD), a progressive neurodegenerative disorder, is characterized by irreversible dopaminergic neuron loss and intra-neuronal a-synuclein aggregation. High mobility group box 1 (HMGB1) has been proven to be involved in autophagy dysfunction induced by a-synuclein accumulation, and the Beclin1-vacuolar protein sorting 34 (Vps34) complex is of great importance to the initiation of autophagy. Nevertheless, the concrete interaction mechanism between HMGB1, a-synuclein and autophagy remains elusive, especially in the context of PD. Here in this study, we investigated the interaction between HMGB1 and a-synuclein in rotenone-induced PD cell models and their roles in autophagy flux. Results revealed elevated expression and cytosolic translocation of endogenous HMGB1 upon rotenone exposure. Besides, HMGB1 was found to be able to co-localize and interact with a-synuclein. Moreover, it had also been proven that HMGB1 could aggravate a-synuclein aggregation induced autophagy dysfunction via perturbing Beclin1-Vps34 complex formation. Based on these findings, we propose that HMGB1 is involved in rotenone-induced dopaminergic cell death via interacting with α-synuclein, perturbing the autophagy process, aggravating protein aggregation and finally propelling dopaminergic neurons to move from morbidity to mortality. [ABSTRACT FROM AUTHOR]
Copyright of Frontiers in Molecular Neuroscience is the property of Frontiers Media S.A. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Label: Title
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  Data: HMGB1 Mediates Autophagy Dysfunction via Perturbing Beclin1-Vps34 Complex in Dopaminergic Cell Model.
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  Data: <searchLink fieldCode="AR" term="%22Jinsha+Huang%22">Jinsha Huang</searchLink><br /><searchLink fieldCode="AR" term="%22Jiaolong+Yang%22">Jiaolong Yang</searchLink><br /><searchLink fieldCode="AR" term="%22Yan+Shen%22">Yan Shen</searchLink><br /><searchLink fieldCode="AR" term="%22Haiyang+Jiang%22">Haiyang Jiang</searchLink><br /><searchLink fieldCode="AR" term="%22Chao+Han%22">Chao Han</searchLink><br /><searchLink fieldCode="AR" term="%22Guoxin+Zhang%22">Guoxin Zhang</searchLink><br /><searchLink fieldCode="AR" term="%22Ling+Liu%22">Ling Liu</searchLink><br /><searchLink fieldCode="AR" term="%22Xiaoyun+Xu%22">Xiaoyun Xu</searchLink><br /><searchLink fieldCode="AR" term="%22Jie+Li%22">Jie Li</searchLink><br /><searchLink fieldCode="AR" term="%22Zhicheng+Lin%22">Zhicheng Lin</searchLink><br /><searchLink fieldCode="AR" term="%22Nian+Xiong%22">Nian Xiong</searchLink><br /><searchLink fieldCode="AR" term="%22Zhentao+Zhang%22">Zhentao Zhang</searchLink><br /><searchLink fieldCode="AR" term="%22Jing+Xiong%22">Jing Xiong</searchLink><br /><searchLink fieldCode="AR" term="%22Tao+Wang%22">Tao Wang</searchLink><br /><searchLink fieldCode="AR" term="%22Carri%2C+Maria+Teresa%22">Carri, Maria Teresa</searchLink><br /><searchLink fieldCode="AR" term="%22Hong+Qing%22">Hong Qing</searchLink>
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  Data: Frontiers in Molecular Neuroscience; 1/31/2017, Vol. 10, p1-11, 11p
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  Data: <searchLink fieldCode="DE" term="%22HIGH+mobility+group+proteins%22">HIGH mobility group proteins</searchLink><br /><searchLink fieldCode="DE" term="%22DOPAMINERGIC+mechanisms%22">DOPAMINERGIC mechanisms</searchLink><br /><searchLink fieldCode="DE" term="%22PARKINSON'S+disease%22">PARKINSON'S disease</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Parkinson's disease (PD), a progressive neurodegenerative disorder, is characterized by irreversible dopaminergic neuron loss and intra-neuronal a-synuclein aggregation. High mobility group box 1 (HMGB1) has been proven to be involved in autophagy dysfunction induced by a-synuclein accumulation, and the Beclin1-vacuolar protein sorting 34 (Vps34) complex is of great importance to the initiation of autophagy. Nevertheless, the concrete interaction mechanism between HMGB1, a-synuclein and autophagy remains elusive, especially in the context of PD. Here in this study, we investigated the interaction between HMGB1 and a-synuclein in rotenone-induced PD cell models and their roles in autophagy flux. Results revealed elevated expression and cytosolic translocation of endogenous HMGB1 upon rotenone exposure. Besides, HMGB1 was found to be able to co-localize and interact with a-synuclein. Moreover, it had also been proven that HMGB1 could aggravate a-synuclein aggregation induced autophagy dysfunction via perturbing Beclin1-Vps34 complex formation. Based on these findings, we propose that HMGB1 is involved in rotenone-induced dopaminergic cell death via interacting with α-synuclein, perturbing the autophagy process, aggravating protein aggregation and finally propelling dopaminergic neurons to move from morbidity to mortality. [ABSTRACT FROM AUTHOR]
– Name: Abstract
  Label:
  Group: Ab
  Data: <i>Copyright of Frontiers in Molecular Neuroscience is the property of Frontiers Media S.A. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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              Text: 1/31/2017
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