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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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...
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Post-translational Translocation of Proteins to the RER01:27

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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
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Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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Tunnels for Protein Export from the Endoplasmic Reticulum.

I Raote1, V Malhotra1,2,3

  • 1Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Barcelona 08003, Spain; email: ishier.raote@crg.eu, vivek.malhotra@crg.eu.

Annual Review of Biochemistry
|January 27, 2021
PubMed
Summary

Metazoans use TANGO1 proteins to create specialized vesicles for exporting large proteins like procollagens from the endoplasmic reticulum. This mechanism complements standard coat protein complex II (COPII) vesicle formation for efficient secretion.

Keywords:
COPIIER exportGolgi complexTANGO1collagentether

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Coat protein complex II (COPII) mediates cargo packaging and vesicle formation at the endoplasmic reticulum, a conserved process in eukaryotic protein secretion.
  • Standard COPII vesicles are insufficient for exporting large, metazoan-specific cargoes, including procollagens, apolipoproteins, and mucins.

Purpose of the Study:

  • To investigate the mechanisms by which metazoans achieve the secretion of large, complex proteins.
  • To elucidate the role of TANGO1 (transport and Golgi organization 1) in facilitating the export of specific cargoes from the endoplasmic reticulum.

Main Methods:

  • Investigated protein interactions between TANGO1 and COPII machinery.
  • Utilized cell-based assays to track the transport of metazoan-specific cargoes.
  • Examined the structural and functional requirements for TANGO1-mediated cargo export.

Main Results:

  • Identified TANGO1 as a key component that bridges COPII coats with early secretory pathway membranes.
  • Demonstrated that TANGO1 enables the formation of specialized export vesicles capable of accommodating large cargoes.
  • Showcased TANGO1's essential role in the secretion of procollagens, apolipoproteins, and mucins.

Conclusions:

  • Metazoans have evolved TANGO1-dependent pathways to overcome the limitations of standard COPII vesicle formation for secreting complex proteins.
  • TANGO1 represents a novel mechanism for cargo export at the endoplasmic reticulum, essential for metazoan-specific secretion.