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Related Concept Videos

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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Role of ER in the Secretory Pathway01:17

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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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Protein Translocation Machinery on the ER Membrane01:28

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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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The Endoplasmic Reticulum01:43

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The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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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.
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Updated: Sep 19, 2025

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

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858

Selenoprotein K Is a Peripheral ER Membrane Protein.

Atinuke Odunsi1, Erfan Rahmani2, Farid Ghelichkhani1

  • 1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.

Biochemistry
|June 5, 2025
PubMed
Summary
This summary is machine-generated.

Selenoprotein K (selenok) is a peripheral, not transmembrane, protein anchored to the ER

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Selenoprotein K (selenok) is a small, disordered ER membrane protein.
  • It plays roles in protein palmitoylation, quality control, calcium homeostasis, migration, and phagocytosis.
  • Selenok has been previously characterized as a single-pass transmembrane protein.

Purpose of the Study:

  • To re-evaluate the membrane topology of selenoprotein K.
  • To compare the topology of selenok with the related selenoprotein S (selenos).

Main Methods:

  • Immunofluorescence microscopy
  • Substituted cysteine accessibility method
  • Selective membrane permeabilization

Main Results:

  • Selenoprotein K is a peripheral membrane protein with both N- and C-termini in the cytoplasm.
  • Selenoprotein S is a transmembrane protein with a cytoplasmic C-terminus and an ER lumen-exposed N-terminus.
  • Selenok's cytoplasmic exposure of termini and amphipathic helix facilitates interactions with cytoplasmic partners.

Conclusions:

  • Selenok's peripheral localization and exposed domains enable interactions with cytoplasmic proteins.
  • This topology is crucial for selenok's function in cellular processes and disease implicated pathways.
  • Findings redefine selenok's role and interaction potential within the ER membrane environment.