Evidence map›Paper›PMID 30999671›Full record

ArticleBiomolecules2019

Membrane Localization of HspA1A, a Stress Inducible 70-kDa Heat-Shock Protein, Depends on Its Interaction with Intracellular Phosphatidylserine.

Andrei D Bilog, Larissa Smulders, Ryan Oliverio, Cedra Labanieh, Julianne Zapanta, Robert V Stahelin, Nikolas Nikolaidis

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

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  10. Interplay between LncRNAs and microRNAs in Breast Cancer.International journal of molecular sciences · 2023
    Review
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  19. Origin and Evolution of the Human Bcl2-Associated Athanogene-1 (BAG-1).International journal of molecular sciences · 2020
    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

7 authors at 2 institutions in 1 country.

Andrei D BilogDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. abilog@fullerton.edu.
Larissa SmuldersDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. l.smulders@csu.fullerton.edu.
Ryan OliverioDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. rolive1011@csu.fullerton.edu.
Cedra LabaniehDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. cedralabanieh@csu.fullerton.edu.
Julianne ZapantaDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. jzap@csu.fullerton.edu.
Robert V StahelinDepartment of Medicinal Chemistry and Molecular Pharmacology and the Purdue University Cancer Center, Purdue University, West Lafayette, IN, 47907, USA. rstaheli@purdue.edu.
Nikolas NikolaidisDepartment of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA. nnikolaidis@fullerton.edu.
California State University, Fullerton · USPurdue University West Lafayette · US

Funding

Interaction between HspA1A, a seventy-kDa heat shock protein, and lipids in stressed cellsSC3GM121226 · NIGMS · CALIFORNIA STATE UNIVERSITY FULLERTON · PI NIKOLAIDIS, NIKOLAS · 2017 to 2024
$843k
NIGMS NIH HHS SC3 GM121226
6 · The paper itself

Abstract

HspA1A is a cytosolic molecular chaperone essential for cellular homeostasis. HspA1A also localizes at the plasma membrane (PM) of tumor and stressed cells. However, it is currently unknown how this cytosolic protein translocates to the PM. Taking into account that HspA1A interacts with lipids, including phosphatidylserine (PS), and that lipids recruit proteins to the PM, we hypothesized that the interaction of HspA1A with PS allows the chaperone to localize at the PM. To test this hypothesis, we subjected cells to mild heat-shock and the PM-localized HspA1A was quantified using confocal microscopy and cell surface biotinylation. These experiments revealed that HspA1A's membrane localization increased during recovery from non-apoptotic heat-shock. Next, we selectively reduced PS targets by overexpressing the C2 domain of lactadherin (Lact-C2), a known PS-biosensor, and determined that HspA1A's membrane localization was greatly reduced. In contrast, the reduction of PI(4,5)P

Indexed as

Cell MembraneHeat-Shock ResponseHEK293 CellsHeLa CellsHSP70 Heat-Shock ProteinsHumansPhosphatidylinositol 4,5-DiphosphatePhosphatidylserinesProtein TransportHSP70 Heat-Shock ProteinsHSPA1A protein, humanPhosphatidylinositol 4,5-DiphosphatePhosphatidylserinesheat-shock proteinslipid–protein interactionsphosphatidylserineplasma membrane

Identifiers

PMID30999671
PMCPMC6523125
OpenAlexW2938708591

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.