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RIPK1 mediates axonal degeneration by promoting inflammation and necroptosis in ALS
Open accessAbstract
Axonal pathology and necroptosis in ALS: Necroptosis, a non–caspase-dependent form of cell death, can be reduced in disease states by inhibiting a kinase called RIPK1. Until now, no human mutations have been linked to necroptosis. Ito et al. show that loss of optineurin, which is encoded by a gene that has been implicated in the human neurodegenerative disorder ALS (amyotrophic lateral sclerosis), results in sensitivity to necroptosis and axonal degeneration. When RIPK1-kinase dependent signaling is disrupted in mice that lack optineurin, necroptosis is inhibited and axonal pathology is reversed. Science , this issue p. 603
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“Moreover, it has recently been reported that the autophagic receptor optineurin (OPTN) [509] actively regulates the proteasomal turnover of RIPK1, as the loss of OPTN induces axonal degeneration via RIPK1-dependent necroptosis [510].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [510]
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“Moreover, it has recently been reported that the autophagic receptor optineurin (OPTN) [509] actively regulates the proteasomal turnover of RIPK1, as the loss of OPTN induces axonal degeneration via RIPK1-dependent necroptosis [510].”
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Metadata
- Authors
- Ito, Y., Ofengeim, D., Najafov, A., Das, S., Saberi, S., Li, Y., Hitomi, J., Zhu, H., Chen, H., Mayo, L., Geng, J., Amin, P., DeWitt, J. P., Mookhtiar, A. K., Florez, M., Ouchida, A. T., Fan, J.-B., Pasparakis, M., Kelliher, M. A., Ravits, J., & Yuan, J.
- Affiliations
- Harvard University (US)
- Massachusetts General Hospital (US)
- Brigham and Women's Hospital (US)
- Illumina (United States) (US)
- University of Cologne (DE)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Yuan, Junying
- ORCID
- Venue
- Science
- Published
- 2016-08-05
- Volume
- 353
- Issue
- 6299
- Pages
- 603-608
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5444917
- OpenAlex
- W2500850723
- Cited by
- 606
- References
- 40
- Citations by year
- 2026: 43 · 2025: 59 · 2024: 66 · 2023: 74 · 2022: 58 · 2021: 79 · 2020: 74 · 2019: 57 · 2018: 55 · 2017: 33 · 2016: 6
- FWCI
- 38.10
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (1R01NS082257)
- National Institute on Aging (1R01AG047231)
- NIH
- National Science and Technology Major Project of China (2014ZX09102001-002)
- State Key Program of National Natural Science of China (31530041)
- National Institute of Allergy and Infectious Diseases (2RO1AI075118)
- European Research Council (323040)
- Daiichi Sankyo Foundation of Life Science
- The Nakatomi Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Japan Society for the Promotion of Science
- National Multiple Sclerosis Society
- National Multiple Sclerosis Society Career Transition Award
- Huazhong University of Science and Technology
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- amyotrophic lateral sclerosis, optineurin, RIPK1, RIPK3, MLKL, necroptosis, axonal degeneration, neuroinflammation, dysmyelination, SOD1 G93A mice, axonal protection
- MeSH terms
- Superoxide Dismutase-1, Amyotrophic Lateral Sclerosis, Animals, Axons, Humans, Inflammation, Mice, Transgenic, Necrosis, Nerve Degeneration, Spinal Cord, Superoxide Dismutase, Suppression, Genetic, Apoptosis, Cell Cycle Proteins, Membrane Transport Proteins, Transcription Factor TFIIIA, Mice, Receptor-Interacting Protein Serine-Threonine Kinases
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