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Related Concept Videos

Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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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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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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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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Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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Confocal and Super-Resolution Imaging of Polarized Intracellular Trafficking and Secretion of Basement Membrane Proteins During Drosophila Oogenesis
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Fluorogenic Probing of Membrane Protein Trafficking.

Chenge Li1, Aurélien Mourton2,3, Marie-Aude Plamont1

  • 1PASTEUR, Département de Chimie, École Normale Supérieure , PSL University, Sorbonne Université, CNRS , 75005 Paris , France.

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Summary

Researchers developed a new method for fluorescently labeling cell-surface membrane proteins using the FAST tag and HBR analogs. This technique enables efficient study of protein trafficking and potential drug screening for related diseases.

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Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Understanding membrane protein function and trafficking is crucial in cell biology.
  • Existing methods for labeling cell-surface and intracellular proteins can be complex or lack selectivity.

Purpose of the Study:

  • To develop an efficient strategy for the rapid and selective fluorescent labeling of membrane proteins.
  • To enable the study of protein trafficking at the plasma membrane.
  • To facilitate high-throughput screening for drugs targeting protein trafficking defects.

Main Methods:

  • Utilized the chemical-genetic fluorescent marker FAST (fluorescence-activating and absorption-shifting tag).
  • Employed fluorogenic membrane-impermeant 4-hydroxybenzylidene rhodanine (HBR) analogs for selective labeling.
  • Applied fluorometric techniques to study protein trafficking.

Main Results:

  • Demonstrated an efficient strategy for rapid and selective fluorescent labeling of cell-surface FAST-tagged proteins.
  • Showcased the ability to study protein trafficking at the plasma membrane.
  • Opened prospects for high-throughput screening of small molecules.

Conclusions:

  • The FAST tag and HBR analog system provides a powerful tool for studying membrane protein trafficking.
  • This approach has significant implications for understanding and potentially treating diseases related to protein trafficking defects.