Evidence map›Paper›PMID 31729431›Full record

ArticleScientific reports2019

Unconventional secretion of α-Crystallin B requires the Autophagic pathway and is controlled by phosphorylation of its serine 59 residue.

M D'Agostino, G Scerra, M Cannata Serio, M G Caporaso, S Bonatti, M Renna

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Unconventional secretion of PARK7 requires lysosomal delivery via chaperone-mediated autophagy and specialized SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Journal of medicinal chemistry · 2023
    Article
  13. Article
  14. Clusterin, other extracellular chaperones, and eye disease.Progress in retinal and eye research · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Autophagy-Related Pathways in Vesicular Unconventional Protein Secretion.Frontiers in cell and developmental biology · 2022
    Review
  19. Article
  20. Article
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

6 authors at 2 institutions in 2 countries.

M D'AgostinoDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Naples, Italy. massimo.dagostino@unina.it.
G ScerraDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Naples, Italy.
M Cannata SerioLaboratory of Epithelial Biology and Disease, Imagine Institute, Paris, France.
M G CaporasoDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Naples, Italy.
S BonattiDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Naples, Italy.ORCID http://orcid.org/0000-0002-7303-0644
M RennaDepartment of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Naples, Italy. maurizio.renna@unina.it.
University of Naples Federico II · ITDélégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Crystallin B (CRYAB or HspB5) is a chaperone member of the small heat-shock protein family that prevents aggregation of many cytosolic client proteins by means of its ATP-independent holdase activity. Surprisingly, several reports show that CRYAB exerts a protective role also extracellularly, and it has been recently demonstrated that CRYAB is secreted from human retinal pigment epithelial cells by an unconventional secretion pathway that involves multi-vesicular bodies. Here we show that autophagy is crucial for this unconventional secretion pathway and that phosphorylation at serine 59 residue regulates CRYAB secretion by inhibiting its recruitment to the autophagosomes. In addition, we found that autophagosomes containing CRYAB are not able to fuse with lysosomes. Therefore, CRYAB is capable to highjack and divert autophagosomes toward the exocytic pathway, inhibiting their canonical route leading to the lysosomal compartment. Potential implications of these findings in the context of disease-associated mutant proteins turn-over are discussed.

Indexed as

alpha-Crystallin B ChainAnimalsAutophagosomesAutophagyChlorocebus aethiopsCOS CellsExtracellular Signal-Regulated MAP KinasesHeLa CellsHumansIntracellular Signaling Peptides and ProteinsLysosomesMAP-Kinase-Activated Kinase 2Mutant ProteinsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine Kinasesalpha-Crystallin B ChainCRYAB protein, humanExtracellular Signal-Regulated MAP KinasesIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2MAP-kinase-activated kinase 3Mutant ProteinsProtein Serine-Threonine KinasesSerine

Identifiers

PMID31729431
PMCPMC6858465
OpenAlexW2988880905

What OpenQuestion holds

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LicenceCC BY
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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.