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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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...
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SNAREs and Membrane Fusion01:43

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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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
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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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Regulation of Nuclear Protein Sorting01:45

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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.
Sec61 protein conducting channel
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Updated: Sep 1, 2025

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Rerouting trafficking circuits through posttranslational SNARE modifications.

Harry Warner1, Shweta Mahajan2, Geert van den Bogaart1

  • 1Department of Molecular Immunology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.

Journal of Cell Science
|August 16, 2022
PubMed
Summary
This summary is machine-generated.

Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) regulate membrane trafficking. Post-translational modifications (PTMs) like phosphorylation and ubiquitylation reprogramme SNARE function, providing cells with plasticity to adapt to environmental changes.

Keywords:
Membrane trafficPosttranslational modificationsSNARE proteins

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Area of Science:

  • Cell biology
  • Molecular biology
  • Membrane trafficking

Background:

  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are crucial for membrane fusion and trafficking.
  • SNAREs mediate vesicle transport by forming complexes between Q-SNAREs and R-SNAREs.
  • The regulation of SNARE function through post-translational modifications (PTMs) is an emerging area of research.

Purpose of the Study:

  • To review current knowledge on how PTMs regulate SNARE protein function.
  • To discuss the role of SNARE PTMs in cellular adaptation and membrane traffic reprogramming.
  • To highlight the functional plasticity conferred by SNARE PTMs.

Main Methods:

  • Literature review of proteomic studies and functional analyses.
  • Summary of established SNARE complex formation and dissociation mechanisms.
  • Discussion of specific PTMs including phosphorylation and ubiquitylation.

Main Results:

  • Proteomic studies confirm SNAREs undergo various PTMs, including phosphorylation and ubiquitylation.
  • PTMs are increasingly recognized as key regulators of SNARE localization and function.
  • SNARE PTMs enable dynamic control over membrane trafficking pathways.

Conclusions:

  • PTMs provide significant functional plasticity to SNARE proteins.
  • SNARE PTMs allow cells to rapidly adjust membrane traffic in response to extracellular cues.
  • Understanding SNARE PTMs is critical for deciphering cellular responses and membrane dynamics.