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Related Concept Videos

GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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GPCR Desensitization01:12

GPCR Desensitization

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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Related Experiment Video

Updated: Apr 3, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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Chaperone gp96 mediates ER-α36 cell membrane expression.

Junwei Hou1, Mengmeng Deng1, Xin Li1

  • 1CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing 100101, P.R. China.

Oncotarget
|September 24, 2015
PubMed
Summary

Cell membrane glycoprotein 96 (mgp96) stabilizes estrogen receptor-alpha 36 (ER-α36), promoting breast cancer growth. Targeting mgp96 inhibits tumor progression, offering a potential therapeutic strategy for ER-α36-overexpressing breast cancers.

Keywords:
ER-α36MAPKbreast cancergp96ubiquitin

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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
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Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Signaling

Background:

  • Estrogen receptor-alpha 36 (ER-α36), a variant of ERα, activates non-genomic pathways and is implicated in breast cancer growth and tamoxifen resistance.
  • The precise mechanisms regulating cell membrane expression of ER-α36 remain largely unelucidated.

Purpose of the Study:

  • To investigate the role of cell membrane glycoprotein 96 (mgp96) in regulating ER-α36 expression and signaling in breast cancer.
  • To explore the potential of targeting the mgp96-ER-α36 interaction as a therapeutic strategy.

Main Methods:

  • Investigated the direct interaction between mgp96 and ER-α36 on the cell membrane of breast tumor cells.
  • Utilized siRNA and monoclonal antibody (mAb) to target mgp96 in vitro and in vivo models.
  • Assessed the impact on ER-α36 stabilization, signaling, tumor cell growth, and invasion.

Main Results:

  • The C-terminal domain of mgp96 directly interacts with and stabilizes cell membrane ER-α36 in breast tumor cells.
  • This interaction enhances ER-α36 signaling, leading to increased tumor cell growth and invasion.
  • Targeting mgp96 effectively blocked the interaction and inhibited breast cancer progression both in vitro and in vivo.

Conclusions:

  • mgp96 plays a critical role in modulating cell membrane ER-α36 expression and promoting breast cancer development.
  • mgp96 represents a promising therapeutic target for ER-α36-overexpressing breast cancers.