The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway
Open accessAbstract
Hexanucleotide repeat expansion in the C9orf72 gene is a leading cause of frontotemporal lobar degeneration (FTLD) with amyotrophic lateral sclerosis (ALS). Reduced expression of C9orf72 has been proposed as a possible disease mechanism. However, the cellular function of C9orf72 remains to be characterized. Here we report the identification of two binding partners of C9orf72: SMCR8 and WDR41. We show that WDR41 interacts with the C9orf72/SMCR8 heterodimer and WDR41 is tightly associated with the Golgi complex. We further demonstrate that C9orf72/SMCR8/WDR41 associates with the FIP200/Ulk1 complex, which is essential for autophagy initiation. C9orf72 deficient mice, generated using the CRISPR/Cas9 system, show severe inflammation in multiple organs, including lymph node, spleen and liver. Lymph node enlargement and severe splenomegaly are accompanied with macrophage infiltration. Increased levels of autophagy and lysosomal proteins and autophagy defects were detected in both the spleen and liver of C9orf72 deficient mice, supporting an in vivo role of C9orf72 in regulating the autophagy/lysosome pathway. In summary, our study elucidates potential physiological functions of C9orf72 and disease mechanisms of ALS/FTLD.
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C9orf72 forms a complex with SMCR8 and WDR41, which targets the complex to lysosomes and interacts with RB1CC1-ULK1-ATG13-ATG101 to regulate autophagosome formation.
“C9orf72 also forms a complex with SMCR8, a guanine nucleotide exchange factor, and WDR41, a WD40 protein essential for targeting the C9orf72-SMCR8-WDR41 complex to lysosomes [146–150]. Here, this complex interacts with RB1CC1-ULK1-ATG13-ATG101, which together are involved in autophagosome formation [149].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [149]
C9orf72 deficiency leads to lymphocytic inflammation, lymphadenopathy, and splenomegaly.
“C9orf72 deficiency leads to lymphocytic inflammation, lymphadenopathy, and splenomegaly [149]”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [149]
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- Authors
- Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F.
- Affiliations
- Cornell University (US)
- Corresponding author
- Hu, Fenghua
- Venue
- Acta Neuropathologica Communications
- Published
- 2016-05-18
- Volume
- 4
- Issue
- 1
- Pages
- 51-51
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC4870812
- OpenAlex
- W2406553940
- Cited by
- 295
- References
- 57
- Citations by year
- 2026: 13 · 2025: 20 · 2024: 16 · 2023: 30 · 2022: 20 · 2021: 46 · 2020: 36 · 2019: 29 · 2018: 37 · 2017: 32 · 2016: 15 · 2015: 1
- FWCI
- 28.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association (255396)
- National Institute of Neurological Disorders and Stroke (R01NS088448-01)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- C9orf72, SMCR8, hexanucleotide repeat expansion, amyotrophic lateral sclerosis, frontotemporal lobar degeneration, autophagy-lysosome pathway, Golgi apparatus, protein-protein interaction, splenomegaly, lymphadenopathy, macrophage infiltration, lysosomal proteins
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein-1 Homolog, C9orf72 Protein, Amyotrophic Lateral Sclerosis, Animals, Autophagy, Carrier Proteins, HeLa Cells, Humans, Liver, Lymph Nodes, Lysosomes, Protein Binding, Protein-Tyrosine Kinases, Proteins, Spleen, Mice, Knockout, Guanine Nucleotide Exchange Factors, Intracellular Signaling Peptides and Proteins, Protein Multimerization, Frontotemporal Lobar Degeneration, HEK293 Cells, CRISPR-Cas Systems
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