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Autophagy Volume 15, 2019 - Issue 4
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Research Paper

The cargo receptor SQSTM1 ameliorates neurofibrillary tangle pathology and spreading through selective targeting of pathological MAPT (microtubule associated protein tau)

Yin XuHuffington Center on Aging, Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USAView further author information
,
Sheng ZhangThe Brown Foundation Institute of Molecular Medicine, Department of Neurobiology and Anatomy, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX, USAORCID Iconhttp://orcid.org/0000-0001-6015-2960View further author information
ORCID Icon &
Hui ZhengHuffington Center on Aging, Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USACorrespondence[email protected]
ORCID Iconhttp://orcid.org/0000-0002-5427-3798View further author information
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Pages 583-598 | Received 27 Nov 2017, Accepted 26 Sep 2018, Published online: 16 Oct 2018

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Heng Lin, Sarah Sandkuhler, Colleen Dunlea, Joel Rodwell-Bullock, Darron H King & Gail V. W. Johnson. (2023) BAG3 regulates the specificity of the recognition of specific MAPT species by NBR1 and SQSTM1. Autophagy 0:0, pages 1-13.
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Celine Deneubourg, Mauricio Ramm, Luke J. Smith, Olga Baron, Kritarth Singh, Susan C. Byrne, Michael R. Duchen, Mathias Gautel, Eeva-Liisa Eskelinen, Manolis Fanto & Heinz Jungbluth. (2022) The spectrum of neurodevelopmental, neuromuscular and neurodegenerative disorders due to defective autophagy. Autophagy 18:3, pages 496-517.
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Cenxiao Fang, Jung-A A. Woo, Tian Liu, Xingyu Zhao, Sara Cazzaro, Yan Yan, Jenet Matlack, Teresa Kee, Patrick LePochat & David E. Kang. (2021) SSH1 impedes SQSTM1/p62 flux and MAPT/Tau clearance independent of CFL (cofilin) activation. Autophagy 17:9, pages 2144-2165.
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Bernd Bauer, Sascha Martens & Luca Ferrari. (2023) Aggrephagy at a glance. Journal of Cell Science 136:10.
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Hilary Grosso Jasutkar & Ai Yamamoto. (2023) Autophagy at the synapse, an early site of dysfunction in neurodegeneration. Current Opinion in Physiology 32, pages 100631.
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Yuxin Zhou, Yongqi Zhen, Guan Wang & Bo Liu. (2022) Deconvoluting the Complexity of Reactive Oxygen Species (ROS) in Neurodegenerative Diseases. Frontiers in Neuroanatomy 16.
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Yin Xu, Yun Liu, Xi Chen, Qia Xu, Liwei Liu, Hui Liu, Ruowen Guo & Yide Qin. (2022) OPTN attenuates the neurotoxicity of abnormal Tau protein by restoring autophagy. Translational Psychiatry 12:1.
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Jing Zuo, Zhe Zhang, Maochao Luo, Li Zhou, Edouard C. Nice, Wei Zhang, Chuang Wang & Canhua Huang. (2022) Redox signaling at the crossroads of human health and disease. MedComm 3:2.
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Zhiqiang Deng, Yu Dong, Xiaoting Zhou, Jia-Hong Lu & Zhenyu Yue. (2022) Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles. Acta Pharmaceutica Sinica B 12:4, pages 1688-1706.
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Jung-AA Woo, Yan Yan, Teresa R Kee, Sara Cazzaro, Kyle C McGill Percy, Xinming Wang, Tian Liu, Stephen B Liggett & David E Kang. (2022) β-arrestin1 promotes tauopathy by transducing GPCR signaling, disrupting microtubules and autophagy. Life Science Alliance 5:3, pages e202101183.
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Yin Xu, Shuqi Du, Jacob A. Marsh, Kanta Horie, Chihiro Sato, Andrea Ballabio, Celeste M. Karch, David M. Holtzman & Hui Zheng. (2020) TFEB regulates lysosomal exocytosis of tau and its loss of function exacerbates tau pathology and spreading. Molecular Psychiatry 26:10, pages 5925-5939.
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Jessica Root, Paola Merino, Austin Nuckols, Michelle Johnson & Thomas Kukar. (2021) Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis. Neurobiology of Disease 154, pages 105360.
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Hyungsun Park, Ju-Hee Kang & Seongju Lee. (2020) Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates. International Journal of Molecular Sciences 21:9, pages 3369.
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Katarzyna Zientara-Rytter & Suresh Subramani. (2019) The Roles of Ubiquitin-Binding Protein Shuttles in the Degradative Fate of Ubiquitinated Proteins in the Ubiquitin-Proteasome System and Autophagy. Cells 8:1, pages 40.
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