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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
ER Retrieval Pathway01:45

ER Retrieval Pathway

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...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...

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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

RET(MEN 2B) is active in the endoplasmic reticulum before reaching the cell surface.

P Runeberg-Roos1, H Virtanen, M Saarma

  • 1Institute of Biotechnology, Viikki Biocenter, University of Helsinki, Helsinki, Finland. pia.runeberg@helsinki.fi

Oncogene
|June 30, 2007
PubMed
Summary

Multiple endocrine neoplasia type 2B (MEN 2B) involves an abnormal RET receptor tyrosine kinase. The MEN 2B precursor activates signaling pathways from the endoplasmic reticulum, even before reaching the cell surface.

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Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • Multiple Endocrine Neoplasia type 2B (MEN 2B) is an autosomal dominant cancer syndrome.
  • It is caused by an oncogenic form of the REarranged during transfection (RET) receptor tyrosine kinase.
  • MEN 2B is characterized by abnormal, ligand-independent autophosphorylation of the mutated RET receptor.

Purpose of the Study:

  • To characterize the activation of the RET(MEN 2B) variant with the Met918Thr mutation.
  • To investigate the phosphorylation and signaling capabilities of the RET(MEN 2B) precursor in the endoplasmic reticulum (ER).

Main Methods:

  • Characterization of RET(MEN 2B) variant phosphorylation during synthesis in the ER.
  • Analysis of RET(MEN 2B) precursor interactions with adapter proteins (GRB2, SHC) in the ER.
  • Assessment of downstream signaling (AKT, ERK, STAT3) activation by ER-localized RET mutants.

Main Results:

  • The RET(MEN 2B) precursor is phosphorylated on multiple tyrosine residues (Tyr905, Tyr1062, Tyr1096) during synthesis in the ER.
  • The RET(MEN 2B) precursor interacts with GRB2 and SHC in the ER in a kinase activity-dependent manner.
  • ER-localized RET(MEN 2B) precursor activates AKT, ERK, and STAT3 signaling pathways.

Conclusions:

  • The oncogenic RET(MEN 2B) precursor is phosphorylated and interacts with adapter proteins within the ER.
  • Downstream signaling is initiated from the ER by the oncogenic RET(MEN 2B) precursor, preceding its cell surface arrival.