ArticleProteins2014
Intrinsically disordered regions in autophagy proteins.
Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 2 of them syntheses that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
53 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).Autophagy · 2016Guideline
- A New Anatomy of Autophagic Clearance: On the Roles of Intrinsic Disorder in the Membrane-Less on Membrane-Encapsulated Mechanism.Membranes · 2026Review
- Pellino 3 E3 ligase promotes starvation-induced autophagy to prevent hepatic steatosis.Science advances · 2025Article
- Structural insights into Beclin 1 interactions with it's regulators for autophagy modulation.Computational and structural biotechnology journal · 2025Review
- Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- ULK/Atg1: phasing in and out of autophagy.Trends in biochemical sciences · 2024Review
- Invariant BECN1 CXXC motifs bind ZnAutophagy · 2024Article
- Ksp1 is an autophagic receptor protein for the Snx4-assisted autophagy of Ssn2/Med13.Autophagy · 2024Article
- Epstein-Barr Virus Encoded BCL2, BHRF1, Downregulates Autophagy by Noncanonical Binding of BECN1.Biochemistry · 2023Article
- The Intrinsically Disordered N Terminus in Atg12 from Yeast Is Necessary for the Functional Structure of the Protein.International journal of molecular sciences · 2023Article
- Article
- Ambra1 in cancer: implications for clinical oncology.Apoptosis : an international journal on programmed cell death · 2022Review
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- Phase Separation in Regulation of Autophagy.Frontiers in cell and developmental biology · 2022Article
- AMBRA1 and its role as a target for anticancer therapy.Frontiers in oncology · 2022Review
- Targeting cancer stem cells in medulloblastoma by inhibiting AMBRA1 dual function in autophagy and STAT3 signalling.Acta neuropathologica · 2021Article
- Circular dichroism for secondary structure determination of proteins with unfolded domains using a self-organising map algorithm SOMSpec.RSC advances · 2021Article
- Autophagosome biogenesis comes out of the black box.Nature cell biology · 2021Review
- The crystal structure of Atg18 reveals a new binding site for Atg2 in Saccharomyces cerevisiae.Cellular and molecular life sciences : CMLS · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Autophagy is an essential eukaryotic pathway required for cellular homeostasis. Numerous key autophagy effectors and regulators have been identified, but the mechanism by which they carry out their function in autophagy is not fully understood. Our rigorous bioinformatic analysis shows that the majority of key human autophagy proteins include intrinsically disordered regions (IDRs), which are sequences lacking stable secondary and tertiary structure; suggesting that IDRs play an important, yet hitherto uninvestigated, role in autophagy. Available crystal structures corroborate the absence of structure in some of these predicted IDRs. Regions of orthologs equivalent to the IDRs predicted in the human autophagy proteins are poorly conserved, indicating that these regions may have diverse functions in different homologs. We also show that IDRs predicted in human proteins contain several regions predicted to facilitate protein-protein interactions, and delineate the network of proteins that interact with each predicted IDR-containing autophagy protein, suggesting that many of these interactions may involve IDRs. Lastly, we experimentally show that a BCL2 homology 3 domain (BH3D), within the key autophagy effector BECN1 is an IDR. This BH3D undergoes a dramatic conformational change from coil to α-helix upon binding to BCL2s, with the C-terminal half of this BH3D constituting a binding motif, which serves to anchor the interaction of the BH3D to BCL2s. The information presented here will help inform future in-depth investigations of the biological role and mechanism of IDRs in autophagy proteins.
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Registered trials
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.