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Related Concept Videos

Regulated mRNA Transport02:22

Regulated mRNA Transport

In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing specific...
Regulated mRNA Transport02:22

Regulated mRNA Transport

In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing specific...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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...
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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

Updated: May 28, 2026

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation
14:44

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation

Published on: March 14, 2014

How and why does Dia1 mRNA localize?

Guoning Liao1, Gang Liu

  • 1Center for Cell Biology & Cancer Research; Albany Medical College; Albany, NY USA.

Communicative & Integrative Biology
|November 3, 2011
PubMed
Summary
This summary is machine-generated.

Messenger RNA (mRNA) localization is crucial for cell function. A newly discovered mechanism targets Dia1 mRNA to the endoplasmic reticulum (ER) independently of the previously known zipcode pathway.

Keywords:
IQGAPRhocytoskeletonendoplasmic reticulumformintranslation

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Last Updated: May 28, 2026

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation
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Published on: March 14, 2014

Production of Xenopus tropicalis Egg Extracts to Identify Microtubule-associated RNAs
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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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Intracellular mRNA localization is essential for cellular functions.
  • Two established mechanisms exist: signal peptide-dependent targeting to the ER for secreted proteins, and zipcode-dependent targeting for cytosolic proteins.
  • Recent research identified a novel mRNA targeting pathway.

Purpose of the Study:

  • To discuss the newly identified mechanism for Dia1 mRNA localization.
  • To explore the zipcode-independent targeting of Dia1 mRNA to the perinuclear ER.
  • To investigate the potential physiological significance of this novel pathway.

Main Methods:

  • Analysis of mRNA localization mechanisms.
  • Investigation of protein targeting pathways.
  • Experimental validation of mRNA-protein interactions.

Main Results:

  • A novel mechanism for Dia1 mRNA targeting to the perinuclear ER has been identified.
  • This targeting is independent of the established zipcode pathway.
  • Dia1 mRNA, encoding a cytosolic protein, is directed to the ER via a new route.

Conclusions:

  • The discovery of a zipcode-independent pathway for Dia1 mRNA localization expands our understanding of mRNA transport.
  • This finding suggests alternative mechanisms for regulating protein synthesis spatially within the cell.
  • Further research is needed to fully elucidate the physiological roles of this novel mRNA localization pathway.