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Related Concept Videos

Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
Clathrin Coated Vesicles01:12

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...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

The claudin Megatrachea protein complex.

Martin H J Jaspers1, Kai Nolde, Matthias Behr

  • 1Research Group Molecular Organogenesis, Max Planck Institute for Biophysical Chemistry, Am Fassberg, 37077 Göttingen, Germany.

The Journal of Biological Chemistry
|August 30, 2012
PubMed
Summary
This summary is machine-generated.

This study identifies proteins interacting with the claudin Megatrachea in Drosophila, revealing new components of septate junctions (SJs) and their role in epithelial barriers. Findings suggest Megatrachea

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In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Area of Science:

  • Cell Biology
  • Developmental Biology
  • Molecular Biology

Background:

  • Claudins are essential transmembrane proteins forming tight and septate junctions (SJs), crucial for epithelial barrier function.
  • In Drosophila, claudins are vital for SJ integrity, maintaining epithelial morphogenesis.
  • The molecular interactions and partners of claudins in membrane organization remain largely unexplored.

Purpose of the Study:

  • To comprehensively analyze the claudin proteome in Drosophila.
  • To identify novel proteins interacting with the claudin Megatrachea.
  • To elucidate the role of Megatrachea interactions in SJ function and epithelial organization.

Main Methods:

  • Immunoprecipitation using anti-Megatrachea antibodies followed by mass spectrometry.
  • Proteomic analysis to identify Megatrachea-associated proteins in Drosophila embryos.
  • In vivo functional analysis using tissue-specific RNA interference (RNAi) knockdown.

Main Results:

  • Identified 142 proteins associated with Megatrachea, including known and novel putative SJ components like CG3921.
  • Demonstrated potential involvement of Megatrachea in Sec61p-dependent secretion processes via interaction with Sec61 subunits.
  • Provided evidence that clathrin-coated vesicles may regulate Megatrachea turnover at the plasma membrane.

Conclusions:

  • This study expands the understanding of the claudin interactome in Drosophila, identifying key SJ components.
  • Findings suggest Megatrachea plays a role in regulating secretion and membrane dynamics, analogous to human claudins.
  • The identified proteins represent novel candidates for further investigation in vertebrate and invertebrate claudin-related pathways.