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Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
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Mitsugumin 23 forms a massive bowl-shaped assembly and cation-conducting channel.

Elisa Venturi1, Kazuhiro Mio, Miyuki Nishi

  • 1School of Physiology and Pharmacology, Bristol Heart Institute and Centre for Nanoscience and Quantum Information, University of Bristol, Bristol, United Kingdom.

Biochemistry
|March 9, 2011
PubMed
Summary

Mitsugumin 23 (MG23) forms a voltage-dependent cation channel in intracellular membranes. This transmembrane protein

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Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
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Area of Science:

  • Cell biology
  • Biophysics
  • Membrane protein structure and function

Background:

  • Mitsugumin 23 (MG23) is a 23 kDa transmembrane protein found in ER and nuclear membranes.
  • Its physiological role in intracellular membrane systems remains largely unknown.

Purpose of the Study:

  • To biochemically and biophysically characterize MG23.
  • To elucidate the structure and function of MG23 as an ion channel.

Main Methods:

  • Hydropathicity profiling and limited proteolytic analysis to determine transmembrane segments.
  • Chemical cross-linking to assess oligomeric assembly.
  • Single-particle 3D reconstruction for structural analysis.
  • Reconstitution into planar lipid bilayers to study channel activity.

Main Results:

  • MG23 possesses three transmembrane segments and forms homo-oligomers.
  • Structural analysis revealed a bowl-shaped complex with a central pore.
  • Reconstituted MG23 functions as a voltage-dependent cation channel (K+, Ca2+).
  • MG23 exhibits unusual coordinated gating behavior.

Conclusions:

  • MG23 forms a functional cation channel with a unique gating mechanism.
  • The assembly and disassembly of MG23 complexes may explain its gating behavior.
  • MG23 facilitates rapid cation flux across intracellular membranes.