ArticleThe Journal of biological chemistry2020
NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 24 citations in OpenAlex.
- A Bacterial Effector Hijacks NBR1 to Modulate Both Autophagy and Ubiquitination-Mediated Degradation That Promotes Bacterial Infection.Plant biotechnology journal · 2026Article
- PPP2/PP2A-mediated dephosphorylation of LC3B links PINK1-PRKN/Parkin-mediated mitophagy to SCA12 pathogenesis.Autophagy · 2025Article
- SIK2-mediated phosphorylation of GABARAPL2 facilitates autophagosome-lysosome fusion and rescues neurodegeneration in an Alzheimer's disease model.Translational neurodegeneration · 2025Article
- AlphaFold2 SLiM screen for LC3-LIR interactions in autophagy.Autophagy · 2025Article
- USP19 potentiates autophagic cell death via inhibiting mTOR pathway through deubiquitinating NEK9 in pancreatic cancer.Cell death and differentiation · 2025Article
- Targeting macroautophagy to combat neurodegenerative disease: strategies and considerations.Autophagy reports · 2025Review
- The Mitochondrial Connection: The Nek Kinases' New Functional Axis in Mitochondrial Homeostasis.Cells · 2024Review
- Coordination among frequent genetic variants imparts substance use susceptibility and pathogenesis.Frontiers in neuroscience · 2024Article
- Atg8 family proteins, LIR/AIM motifs and other interaction modes.Autophagy reports · 2023Article
- Post-translational modifications of ATG8 proteins - an emerging mechanism of autophagy control.Journal of cell science · 2023Review
- Inhibition of autophagy; an opportunity for the treatment of cancer resistance.Frontiers in cell and developmental biology · 2023Review
- Regulation of ubiquitin and ubiquitin-like modifiers by phosphorylation.The FEBS journal · 2022Review
- In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022Review
- Review
- Canonical and non-canonical roles for ATG8 proteins in autophagy and beyond.Frontiers in molecular biosciences · 2022Review
- Macroautophagy and aging: The impact of cellular recycling on health and longevity.Molecular aspects of medicine · 2021Review
- LC3B phosphorylation regulates FYCO1 binding and directional transport of autophagosomes.Current biology : CB · 2021Article
- Beyond Autophagy: The Expanding Roles of ATG8 Proteins.Trends in biochemical sciences · 2021Review
- Autophagy and Ciliogenesis.JMA journal · 2021Review
- Towards a better understanding of the neuro-developmental role of autophagy in sickness and in health.Cell stress · 2021Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ATG8 family proteins (ATG8s) are active in all steps of the macroautophagy pathway, and their lipidation is essential for autophagosome formation. Lipidated ATG8s anchored to the outer surface of the phagophore serve as scaffolds for binding of other core autophagy proteins and various effector proteins involved in trafficking or fusion events, whereas those at the inner surface are needed for assembly of selective autophagy substrates. Their scaffolding role depends on specific interactions between the LC3-interacting region (LIR) docking site (LDS) in ATG8s and LIR motifs in various interaction partners. LC3B is phosphorylated at Thr-50 within the LDS by serine/threonine kinase (STK) 3 and STK4. Here, we identified LIR motifs in STK3 and atypical protein kinase Cζ (PKCζ) and never in mitosis A (NIMA)-related kinase 9 (NEK9). All three kinases phosphorylated LC3B Thr-50
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.