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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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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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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...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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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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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
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Related Experiment Video

Updated: Jul 4, 2025

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
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Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions.

Clara Serrano-Novillo1, Irene Estadella1, María Navarro-Pérez1

  • 1Molecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.

Acta Physiologica (Oxford, England)
|January 29, 2024
PubMed
Summary
This summary is machine-generated.

Cardiac Kv7.1 channels and KCNE1 associate at endoplasmic reticulum-plasma membrane junctions (ER-PMjs) before cell surface delivery. Different ER-PMj structures influence Kv7.1 channel function and localization.

Keywords:
ERPMj inducersadaptorscell surface targetingpotassium channels

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Area of Science:

  • Cardiovascular Biology
  • Molecular Cell Biology
  • Ion Channel Physiology

Background:

  • The voltage-gated Kv7.1 channel, with KCNE1, is crucial for cardiac IKs current.
  • Kv7.1 and KCNE1 utilize distinct cellular trafficking pathways to reach the plasma membrane.
  • Kv7.1 localizes to endoplasmic reticulum-plasma membrane junctions (ER-PMjs) before surface expression.

Purpose of the Study:

  • To investigate the targeting mechanisms of Kv7.1 to ER-PMjs.
  • To understand how ER-PMj architecture influences Kv7.1 localization and function.
  • To identify accessory proteins involved in Kv7.1 trafficking and ER-PMj association.

Main Methods:

  • Utilized protein expression analysis, including association and biotinylation assays.
  • Employed advanced microscopy techniques: confocal (immunocytochemistry, FRET, FRAP), dSTORM, and transmission electron microscopy.
  • Integrated proteomics and electrophysiology to assess channel function and interactions.

Main Results:

  • Kv7.1 targets ER-PMjs irrespective of their origin or structure.
  • Kv2.1 and JPHs increase ER-PMj formation, enhancing Kv7.1 cell surface levels.
  • Kv7.1 exhibits differential clustering and interaction with ancillary proteins (VAMPs, AMIGO, VAP B) within distinct ER-PMj structures.

Conclusions:

  • Kv7.1 interacts with diverse ER-PMj structures induced by various mechanisms.
  • The variable architecture of ER-PMjs differentially impacts the trafficking and function of cardiac Kv7.1 channels.
  • Understanding these interactions is key to modulating cardiac electrophysiology.