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Related Concept Videos

Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

81.7K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Membrane Proteins01:30

Membrane Proteins

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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

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Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
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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.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Reverse-topology membrane scission by the ESCRT proteins.

Johannes Schöneberg1, Il-Hyung Lee1, Janet H Iwasa2

  • 1Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA.

Nature Reviews. Molecular Cell Biology
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The endosomal sorting complex required for transport (ESCRT) proteins mediate membrane scission, a crucial step in viral budding and cell division. New cryo-electron microscopy and spectroscopy insights are clarifying the elusive scission mechanism.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Membrane scission, crucial for viral budding, exosome release, and cytokinesis, involves severing membrane necks contiguous with the cytosol.
  • This process, termed 'inverse-topology' membrane scission, is mediated by the endosomal sorting complex required for transport (ESCRT) proteins.
  • While ESCRT assembly and disassembly by vacuolar protein sorting-associated 4 (VPS4) are known, the precise scission mechanism remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of membrane scission mediated by ESCRT proteins.
  • To understand how ESCRT complexes remodel and sever membranes during cellular processes.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to visualize ESCRT complex structures.
  • Various spectroscopic techniques to study protein dynamics and interactions.

Main Results:

  • ESCRT proteins form diverse structures including filaments, spirals, tubes, and conical funnels.
  • These structures are implicated in directing membrane remodeling and facilitating scission.
  • Recent advancements provide new structural and dynamic insights into the scission process.

Conclusions:

  • The study provides critical new insights into the long-standing mystery of ESCRT-mediated membrane scission.
  • Understanding this mechanism has broad implications for viral egress, exosome biogenesis, and cell division.