Evidence map›Paper›PMID 39291732›Full record

ArticleProtein science : a publication of the Protein Society2024

O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone.

Afraah Javed, Oleta T Johnson, Aaron T Balana, Regan F Volk, Andreas Langen, Benjamin S Ahn, Balyn W Zaro, Jason E Gestwicki, Matthew R Pratt

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

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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

9 authors.

Afraah JavedDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Oleta T JohnsonDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Aaron T BalanaDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Regan F VolkDepartment of Pharmaceutical Chemistry and Cardiovascular Research Institute, University of California, San Francisco, California, USA.
Andreas LangenDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Benjamin S AhnDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.
Balyn W ZaroDepartment of Pharmaceutical Chemistry and Cardiovascular Research Institute, University of California, San Francisco, California, USA.
Jason E GestwickiDepartment of Pharmaceutical Chemistry, Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California, USA.ORCID 0000-0002-6125-3154
Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, California, USA.ORCID 0000-0003-3205-5615

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024
$3.1M
Research Training in Chemistry and Chemical BiologyT32GM145460 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jason E Gestwicki · 2022 to 2026
$3.1M
Developing Tools to Probe DnaJB6 Dynamics in Spinobulbular Muscular AtrophyK99NS128717 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JOHNSON, OLETA TANITREA · 2022 to 2022
$119k
National Science FoundationNIGMS NIH HHS R01 GM114537NIGMS NIH HHS T32 GM145460NIH HHS K99NS128717NIH HHS R01GM114537NIH HHS R01NS059690NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

Almost all types of cellular stress induce post-translational O-GlcNAc modifications of proteins, and this increase promotes cell survival. We previously demonstrated that O-GlcNAc on certain small heat shock proteins (sHSPs), including HSP27, directly increases their chaperone activity as one potential protective mechanism. Here, we furthered our use of synthetic proteins to prepare biotinylated sHSPs and show that O-GlcNAc modification of HSP27 also changes how it interacts within the sHSP system and the broader HSP network. Specifically, we show that O-GlcNAc modified HSP27 binds more strongly to the co-chaperone protein BAG3, which then promotes refolding of a model substrate by HSP70. We use proteomics to identify other potential HSP27 interactions that are changed by O-GlcNAc, including one that we confirm with another sHSP, αB-crystallin. These findings add additional evidence for O-GlcNAc as a switch for regulating protein-protein interactions and for modifications of chaperones as one mechanism by which O-GlcNAc protects against protein aggregation.

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsMolecular ChaperonesAcetylglucosaminealpha-Crystallin B ChainHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansProtein BindingProtein Processing, Post-TranslationalProtein RefoldingAcetylglucosamineAdaptor Proteins, Signal Transducingalpha-Crystallin B ChainApoptosis Regulatory ProteinsBAG3 protein, humanHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPB1 protein, humanMolecular Chaperonesaggregationheat shock proteinO‐GlcNAcrefolding

Identifiers

PMID39291732
PMCPMC11409196

What OpenQuestion holds

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LicenceCC BY-NC
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.