Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 14 May 2010

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Membrane
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum Chaperone BiP

Share to Epitopes

Share to Flow Cytometry

Share to Glycosylation

Share to Heat-Shock Proteins

Share to Molecular Chaperones

Source

Open in PubMed Open full text

Identifiers

PMID: 20208072
DOI: 10.1074/jbc.M109.087445
PMCID: PMC2865300

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP.PMID 20208072Read ↗

Characterization and Mechanism of Stress-induced Translocation of 78-Kilodalton Glucose-regulated Protein (GRP78) to the Cell SurfaceSemantic proximity Read ↗

Stress-induced translocation of the endoplasmic reticulum chaperone GRP78/BiP and its impact on human disease and therapySemantic proximity Read ↗

Role of the Unfolded Protein Response Regulator GRP78/BiP in Development, Cancer, and Neurological DisordersSemantic proximity Read ↗

Roles of GRP78 in physiology and cancerSemantic proximity Read ↗

Cancer cells resistant to therapy promote cell surface relocalization of GRP78 which complexes with PI3K and enhances PI(3,4,5)P3 production.Semantic proximity Read ↗

ER residential chaperone GRP78 unconventionally relocalizes to the cell surface via endosomal transport.Semantic proximity Read ↗

Regulation of PERK Signaling and Leukemic Cell Survival by a Novel Cytosolic Isoform of the UPR Regulator GRP78/BiPSemantic proximity Read ↗

Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.Semantic proximity Read ↗

Cell surface GRP78 signaling: An emerging role as a transcriptional modulator in cancerSemantic proximity Read ↗

The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen-activated protein kinase signaling cascades.Semantic proximity Read ↗

The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection.Semantic proximity Read ↗

GRP78/BiP Is Required for Cell Proliferation and Protecting the Inner Cell Mass from Apoptosis during Early Mouse Embryonic DevelopmentSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.