Evidence map›Paper›PMID 20208072›Full record

ArticleThe Journal of biological chemistry2010

Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP.

Yi Zhang, Ren Liu, Min Ni, Parkash Gill, Amy S Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed, 1 pooled it
10.0field-weighted citation impact, top 1% 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

190 citing papers in PubMed, 1 synthesis or guideline pooled it, 326 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  8. Article
  9. Stress-induced translocation of the endoplasmic reticulum chaperone GRP78/BiP and its impact on human disease and therapy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. StarD5 Plays a Critical Role in the Hepatocyte ER Stress Survival Response.International journal of molecular sciences · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Molecular mechanisms that govern infection and antifungal resistance in Mucorales.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  20. Review

130 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Yi ZhangDepartments of Biochemistry and Molecular Biology, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176.
Ren LiuDepartments of Pathology, USC Norris Comprehensive Cancer Center, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176.
Min NiDepartments of Biochemistry and Molecular Biology, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176.
Parkash GillDepartments of Pathology, USC Norris Comprehensive Cancer Center, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176.
Amy S LeeDepartments of Biochemistry and Molecular Biology, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176. Electronic address: amylee@ccnt.usc.edu.
University of Southern California · US

Funding

STRESS INDUCTION OF THE GLUCOSE REGULATED PROTEINSR01CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1985 to 2021
$11.1M
MECHANISM OF ANTI-APOPTOTIC FUNCTION OF GRP78/BiPR01CA111700 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 2005 to 2008
$1.1M
COORDINATED GENE EXPRESSION IN MAMMALIAN CELLSR37CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1988 to 1995
–
NCI NIH HHS CA027607NCI NIH HHS CA111700NCI NIH HHS R01 CA027607NCI NIH HHS R01 CA111700
6 · The paper itself

Abstract

The recent discovery that GRP78/BiP, a typical endoplasmic reticulum (ER) lumenal chaperone, can be expressed on the cell surface, interacting with an increasing repertoire of surface proteins and acting as receptor in signaling pathways, represents a paradigm shift in its biological function. However, the mechanism of GRP78 trafficking from the ER to the cell surface is not well understood. Using a combination of cellular, biochemical, and mutational approaches, we tested multiple hypotheses. Here we report that ER stress actively promotes GRP78 localization on the cell surface, whereas ectopic expression of GRP78 is also able to cause cell surface relocation in the absence of ER stress. Moreover, deletion of the C-terminal ER retention motif in GRP78 alters its cell surface presentation in a dose-dependent manner; however, mutation of the putative O-linked glycosylation site Thr(648) of human GRP78 is without effect. We also identified the exposure of multiple domains of GRP78 on the cell surface and determined that binding of extracellular GRP78 to the cell surface is unlikely. A new topology model for cell surface GRP78 is presented.

Indexed as

Cell LineCell MembraneEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPEpitopesFlow CytometryGlycosylationHeat-Shock ProteinsHumansMolecular ChaperonesMutationPlasmidsEndoplasmic Reticulum Chaperone BiPEpitopesHeat-Shock ProteinsHSPA5 protein, humanMolecular Chaperones

Identifiers

PMID20208072
PMCPMC2865300
OpenAlexW2082073404

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.