Evidence map›Paper›PMID 34836490›Full record

ArticleAutophagy2022

HYPK coordinates degradation of polyneddylated proteins by autophagy.

Debasish Kumar Ghosh, Akash Ranjan

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Emerging mechanisms of ATG8-independent non-canonical autophagy.Journal of physiology and biochemistry · 2026
    Review
  2. Review
  3. Review
  4. Neddylation modification stabilizes LC3B by antagonizing its ubiquitin-mediated degradation and promoting autophagy in skin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024
    Article
  7. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  8. Review
  9. Article
  10. Polymorphism ofIBRO neuroscience reports · 2023
    Article
  11. Article
  12. Frontiers in neuroscience · 2023
    Review
  13. Mutant MESD links cellular stress to type I collagen aggregation in osteogenesis imperfecta type XX.Matrix biology : journal of the International Society for Matrix Biology · 2023
    Article
  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Debasish Kumar GhoshComputational and Functional Genomics Group Centre for Dna Fingerprinting and Diagnostics Uppal Centre for DNA Fingerprinting and Diagnostics, Hyderabad, India.ORCID 0000-0002-9196-0685
Akash RanjanComputational and Functional Genomics Group Centre for Dna Fingerprinting and Diagnostics Uppal Centre for DNA Fingerprinting and Diagnostics, Hyderabad, India.ORCID 0000-0002-4582-1553
Centre for DNA Fingerprinting and Diagnostics · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selective degradation of protein aggregates by macroautophagy/autophagy is an essential homeostatic process of safeguarding cells from the effects of proteotoxicity. Among the ubiquitin-like proteins, NEDD8 conjugation to misfolded proteins is prominent in stress-induced protein aggregates, albeit the function of neddylation in autophagy is unclear. Here, we report that polyneddylation functions as a post-translational modification for autophagic degradation of proteotoxic-stress induced protein aggregates. We also show that HYPK functions as an autophagy receptor in the polyneddylation-dependent aggrephagy. The scaffolding function of HYPK is facilitated by its C-terminal ubiquitin-associated domain and N-terminal tyrosine-type LC3-interacting region which bind to NEDD8 and LC3 respectively. Both NEDD8 and HYPK are positive modulators of basal and proteotoxicity-induced autophagy, leading to protection of cells from protein aggregates, such as aggregates of mutant HTT exon 1. Thus, we propose an indispensable and additive role of neddylation and HYPK in clearance of protein aggregates by autophagy, resulting in cytoprotective effect during proteotoxic stress.

Indexed as

AutophagyCarrier ProteinsTubulinApoptosis Regulatory ProteinsClass III Phosphatidylinositol 3-Kinasesgamma-Aminobutyric AcidGlutamineMicrotubule-Associated ProteinsProtein AggregatesUbiquitinsUbiquitin-Specific ProteasesApoptosis Regulatory ProteinsCarrier ProteinsClass III Phosphatidylinositol 3-Kinasesgamma-Aminobutyric AcidGlutamineHYPK protein, humanMicrotubule-Associated ProteinsProtein AggregatesTubulinUbiquitinsUbiquitin-Specific ProteasesAggrephagyautophagy fluxHTT exon 1 aggregateHYPKNEDD8proteotoxic stress

Identifiers

PMID34836490
PMCPMC9450979
OpenAlexW3217631311

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.