Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β
Amyloid-β (Aβ) plays an important role in Alzheimer’s disease (AD), as oligomeric Aβ induces loss of postsynaptic AMPA receptors (AMPARs) leading to cognitive deficits. The loss of postsynaptic AMPARs is mediated through the clathrin-dependent endocytosis pathway, in which endophilin2 is one of the...
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| Format: | Article |
| Language: | English |
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Wiley
2017-01-01
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| Series: | Neural Plasticity |
| Online Access: | http://dx.doi.org/10.1155/2017/8197085 |
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| author | Jifeng Zhang Yichen Yin Zhisheng Ji Zhenbin Cai Bo Zhao Jiong Li Minghui Tan Guoqing Guo |
| author_facet | Jifeng Zhang Yichen Yin Zhisheng Ji Zhenbin Cai Bo Zhao Jiong Li Minghui Tan Guoqing Guo |
| author_sort | Jifeng Zhang |
| collection | DOAJ |
| description | Amyloid-β (Aβ) plays an important role in Alzheimer’s disease (AD), as oligomeric Aβ induces loss of postsynaptic AMPA receptors (AMPARs) leading to cognitive deficits. The loss of postsynaptic AMPARs is mediated through the clathrin-dependent endocytosis pathway, in which endophilin2 is one of the important regulatory proteins. Endophilin2, which is enriched in both the pre- and postsynaptic membrane, has previously been reported to be important for recycling of synaptic vesicles at the presynaptic membrane. However, the role of endophilin2 in oligomeric Aβ-induced postsynaptic AMPAR endocytosis is not well understood. In this study, we show that endophilin2 does not affect constitutive AMPAR endocytosis. Endophilin2 knockdown, but not overexpression, resisted oligomeric Aβ-induced AMPAR dysfunction. Moreover, endophilin2 colocalized and interacted with GluA1, a subunit of AMPAR, to regulate oligomeric Aβ-induced AMPAR endocytosis. Thus, we have determined a role of endophilin2 in oligomeric Aβ-induced postsynaptic AMPAR dysfunction, indicating possible directions for preventing the loss of AMPARs in cognitive impairment and providing evidence for the clinical treatment of AD. |
| format | Article |
| id | doaj-art-dc14bc7fb1c146d2bb50c733877693eb |
| institution | DOAJ |
| issn | 2090-5904 1687-5443 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Neural Plasticity |
| spelling | doaj-art-dc14bc7fb1c146d2bb50c733877693eb2025-08-20T03:23:57ZengWileyNeural Plasticity2090-59041687-54432017-01-01201710.1155/2017/81970858197085Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-βJifeng Zhang0Yichen Yin1Zhisheng Ji2Zhenbin Cai3Bo Zhao4Jiong Li5Minghui Tan6Guoqing Guo7Department of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Neurology, Guangzhou Red Cross Hospital, Medical College, Jinan University, Guangzhou 510220, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaDepartment of Anatomy, Medical College of Jinan University, Guangzhou 510630, ChinaAmyloid-β (Aβ) plays an important role in Alzheimer’s disease (AD), as oligomeric Aβ induces loss of postsynaptic AMPA receptors (AMPARs) leading to cognitive deficits. The loss of postsynaptic AMPARs is mediated through the clathrin-dependent endocytosis pathway, in which endophilin2 is one of the important regulatory proteins. Endophilin2, which is enriched in both the pre- and postsynaptic membrane, has previously been reported to be important for recycling of synaptic vesicles at the presynaptic membrane. However, the role of endophilin2 in oligomeric Aβ-induced postsynaptic AMPAR endocytosis is not well understood. In this study, we show that endophilin2 does not affect constitutive AMPAR endocytosis. Endophilin2 knockdown, but not overexpression, resisted oligomeric Aβ-induced AMPAR dysfunction. Moreover, endophilin2 colocalized and interacted with GluA1, a subunit of AMPAR, to regulate oligomeric Aβ-induced AMPAR endocytosis. Thus, we have determined a role of endophilin2 in oligomeric Aβ-induced postsynaptic AMPAR dysfunction, indicating possible directions for preventing the loss of AMPARs in cognitive impairment and providing evidence for the clinical treatment of AD.http://dx.doi.org/10.1155/2017/8197085 |
| spellingShingle | Jifeng Zhang Yichen Yin Zhisheng Ji Zhenbin Cai Bo Zhao Jiong Li Minghui Tan Guoqing Guo Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β Neural Plasticity |
| title | Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β |
| title_full | Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β |
| title_fullStr | Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β |
| title_full_unstemmed | Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β |
| title_short | Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor Endocytosis Induced by Oligomeric Amyloid-β |
| title_sort | endophilin2 interacts with glua1 to mediate ampa receptor endocytosis induced by oligomeric amyloid β |
| url | http://dx.doi.org/10.1155/2017/8197085 |
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