Evidence map›Paper›PMID 27641668›Full record

ArticleBiochemical and biophysical research communications2016

Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.

Michela Ciano, Simona Allocca, Maria Camilla Ciardulli, Lucrezia Della Volpe, Stefano Bonatti, Massimo D'Agostino

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

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  14. Panorama of the distal myopathies.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2020
    Review
  15. Article
  16. Reductive Stress-Induced Mitochondrial Dysfunction and Cardiomyopathy.Oxidative medicine and cellular longevity · 2020
    Review
  17. Article
  18. Effects of Long-Term Citrate Treatment in the PC3 Prostate Cancer Cell Line.International journal of molecular sciences · 2019
    Article
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Michela CianoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Simona AlloccaDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Maria Camilla CiardulliDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Lucrezia Della VolpeDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Stefano BonattiDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy. Electronic address: bonatti@unina.it.
Massimo D'AgostinoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
University of Naples Federico II · IT

Funding

Telethon GGP14002
6 · The paper itself

Abstract

We have previously shown that αB-crystallin (CRYAB), a small heat shock protein (sHsp) that prevents irreversible aggregation of unfolded protein by an ATP-independent chaperone activity, plays a pivotal role in the biogenesis of multipass transmembrane proteins (TMPs) assisting their folding from the cytosolic side of the endoplasmic reticulum (ER) (D'Agostino et al., 2013). Here we present evidence, based on phosphomimetic substitutions, that the three phosphorytable serine residues at position 19, 45 and 59 of CRYAB play a different regulatory role in this novel chaperone activity: S19 and S45 have a strong inhibitory effect, either alone or in combination, while S59 has not and counteracts the inhibition caused by single phosphomimetic substitutions at S19 and S45. Interestingly, all phosphomimetic substitutions determine the formation of smaller oligomeric complexes containing CRYAB, indicating that the inhibitory effect seen for S19 and S45 cannot be ascribed to the reduction of oligomerization frequently associated to a decreased chaperone activity. These results indicate that phosphorylation finely regulates the chaperone activity of CRYAB with multipass TMPs and suggest a pivotal role for S59 in this process.

Indexed as

alpha-Crystallin B ChainCell Line, TumorDNA, ComplementaryGreen Fluorescent ProteinsHumansMembrane ProteinsMolecular ChaperonesMutagenesisMutationPhosphorylationPlasmidsProtein BindingProtein FoldingSerineSignal Transductionalpha-Crystallin B ChainDNA, ComplementaryGreen Fluorescent ProteinsMembrane ProteinsMolecular ChaperonesSerineChaperone activityMultipass transmembrane proteinsPhosphorylationαB-crystallin/HspB5/CRYAB

Identifiers

PMID27641668
PMCPMC5053547
OpenAlexW2520748429

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.