Evidence map›Paper›PMID 20410136›Full record

ArticleMolecular biology of the cell2010

BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells.

Chun Wei Lai, Deborah E Aronson, Erik Lee Snapp

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Coordinated expression and assembly of BiP, p58Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
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  8. Review
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  12. Review
  13. Article
  14. ER chaperone GRP78/BiP translocates to the nucleus under stress and acts as a transcriptional regulator.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  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

3 authors at 1 institution in 1 country.

Chun Wei LaiDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Deborah E Aronson
Erik Lee Snapp
Albert Einstein College of Medicine · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
TRAINING PROGRAM IN CELLULAR &MOLEC. BIOLOGY &GENETICST32GM007491 · NIGMS · YESHIVA UNIVERSITY · PI QUERY, CHARLES C · 1985 to 2021
$17.0M
ER Chaperone Availability in Cells During Homeostasis and Misfolded Protein StresR01GM086530 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SNAPP, ERIK L. · 2009 to 2010
$638k
DETECTING AND RESPONDING TO MISFOLDED PROTEIN BURDENS IN AGING CELLSR21AG032544 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SCHMIDT, MARION, SNAPP, ERIK L. · 2008 to 2009
$457k
Mechanism of Targeting of a Luminal KDEL-containing Protein to the Golgi ComplexF31GM089090 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI ARONSON, DEBORAH · 2009 to 2010
$83k
NIA NIH HHS R21 1R21AG032544-01NIA NIH HHS R21 AG032544NIGMS NIH HHS F31 GM089090NIGMS NIH HHS F31GM089090NIGMS NIH HHS R01 GM086530NIGMS NIH HHS R01GM086530-01NIGMS NIH HHS T32 GM007288NIGMS NIH HHS T32 GM007491NIGMS NIH HHS T32GM07288
6 · The paper itself

Abstract

Accumulation of misfolded secretory proteins causes cellular stress and induces the endoplasmic reticulum (ER) stress pathway, the unfolded protein response (UPR). Although the UPR has been extensively studied, little is known about the molecular changes that distinguish the homeostatic and stressed ER. The increase in levels of misfolded proteins and formation of complexes with chaperones during ER stress are predicted to further crowd the already crowded ER lumen. Surprisingly, using live cell fluorescence microscopy and an inert ER reporter, we find the crowdedness of stressed ER, treated acutely with tunicamycin or DTT, either is comparable to homeostasis or significantly decreases in multiple cell types. In contrast, photobleaching experiments revealed a GFP-tagged variant of the ER chaperone BiP rapidly undergoes a reversible quantitative decrease in diffusion as misfolded proteins accumulate. BiP mobility is sensitive to exceptionally low levels of misfolded protein stressors and can detect intermediate states of BiP availability. Decreased BiP availability temporally correlates with UPR markers, but restoration of BiP availability correlates less well. Thus, BiP availability represents a novel and powerful tool for reporting global secretory protein misfolding levels and investigating the molecular events of ER stress in single cells, independent of traditional UPR markers.

Indexed as

HomeostasisStress, PhysiologicalAnimalsCell LineCell SurvivalCricetinaeEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGenes, ReporterGreen Fluorescent ProteinsHeat-Shock ProteinsHumansProtein FoldingRecombinant Fusion ProteinsTransfectionViscosityEndoplasmic Reticulum Chaperone BiPGreen Fluorescent ProteinsHeat-Shock ProteinsRecombinant Fusion Proteins

Identifiers

PMID20410136
PMCPMC2883936
OpenAlexW2144750503

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.