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Related Concept Videos

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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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.
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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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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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
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Membrane protein biogenesis by the EMC.

Sara Alvira1, Robin A Corey2, Ian Collinson1

  • 1School of Biochemistry, University of Bristol, Bristol, UK.

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The endoplasmic reticulum membrane protein complex (EMC) helps insert hydrophobic proteins into the ER. Recent structural studies reveal the mechanisms behind this essential cellular process.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • The endoplasmic reticulum (ER) membrane protein complex (EMC) is crucial for protein homeostasis.
  • The EMC facilitates the insertion of transmembrane domains (TMDs) into the ER membrane.
  • Understanding the EMC's function is vital for comprehending protein biogenesis.

Discussion:

  • Recent advancements in cryo-electron microscopy (cryo-EM) have provided high-resolution structures of the EMC.
  • These structures, along with other models, offer insights into the EMC's mechanism of action.
  • Understanding this mechanism is key to comprehending how proteins are correctly integrated into the ER membrane.

Key Insights:

  • The EMC facilitates the insertion of challenging transmembrane domains.
  • Structural data elucidates the molecular machinery involved in this process.
  • This research sheds light on a fundamental aspect of protein biogenesis.

Outlook:

  • Further structural and functional studies will refine our understanding of the EMC.
  • Investigating the EMC's role in disease could reveal new therapeutic targets.
  • The findings pave the way for exploring other membrane protein insertion machineries.