Evidence map›Paper›PMID 9724719›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane.

I U Khan, R Wallin, R S Gupta, G M Kammer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 114 citations in OpenAlex.

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  19. Surface architecture of histoplasma capsulatum.Frontiers in microbiology · 2011
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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

4 authors at 1 institution in 2 countries.

I U KhanDepartment of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, N. C. 27157, Canada.
R Wallin
R S Gupta
G M Kammer
McMaster University · CA

Funding

Tumor Tissue CoreP30CA012197 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Ruben A. Mesa · 1985 to 2026
$55.4M
T LYMPHOCYTE DYSFUNCTION IN LUPUS ERYTHEMATOSUSR01AR039501 · NIAMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI KHAN, ISLAM U · 1988 to 2006
$2.7M
NCI NIH HHS 5 P30 CA12197-21N,21S1NCI NIH HHS CA-12197-22NCI NIH HHS P30 CA012197NIAMS NIH HHS AR-39501NIAMS NIH HHS R01 AR039501
6 · The paper itself

Abstract

Accumulating evidence suggests that the mitochondrial molecular chaperone heat shock protein 60 (hsp60) also can localize in extramitochondrial sites. However, direct evidence that hsp60 functions as a chaperone outside of mitochondria is presently lacking. A 60-kDa protein that is present in the plasma membrane of a human leukemic CD4(+) CEM-SS T cell line and is phosphorylated by protein kinase A (PKA) was identified as hsp60. An 18-kDa plasma membrane-associated protein coimmunoprecipitated with hsp60 and was identified as histone 2B (H2B). Hsp60 physically associated with H2B when both molecules were in their dephospho forms. By contrast, PKA-catalyzed phosphorylation of both hsp60 and H2B caused dissociation of H2B from hsp60 and loss of H2B from the plasma membrane of intact T cells. These results suggest that (i) hsp60 and H2B can localize in the T cell plasma membrane; (ii) hsp60 functions as a molecular chaperone for H2B; and (iii) PKA-catalyzed phosphorylation of both hsp60 and H2B appears to regulate the attachment of H2B to hsp60. We propose a model in which phosphorylation/dephosphorylation regulates chaperoning of H2B by hsp60 in the plasma membrane.

Indexed as

Amino Acid SequenceCatalysisCD4-Positive T-LymphocytesCell MembraneChaperonin 60Cyclic AMP-Dependent Protein KinasesHistonesHumansMass SpectrometryMicroscopy, ConfocalMicroscopy, FluorescenceMolecular Sequence DataPeptide MappingPhosphorylationPrecipitin TestsRecombinant ProteinsChaperonin 60Cyclic AMP-Dependent Protein KinasesHistonesRecombinant Proteins

Identifiers

PMID9724719
PMCPMC27910
OpenAlexW2079726240

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.