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Related Concept Videos

Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
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Autophagic Cell Death

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Gap Junctions01:37

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Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Gap Junctions01:27

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The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles
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Internalized gap junctions are degraded by autophagy.

John T Fong1, Rachael M Kells, Anna M Gumpert

  • 1Department of Biological Sciences, Lehigh University, Bethlehem, PA, USA.

Autophagy
|May 29, 2012
PubMed
Summary

This study reveals that internalized gap junctions (GJs) are degraded via autophagy, a cellular recycling process. The protein p62 targets these GJs for degradation, uncovering a novel pathway for GJ turnover and cellular communication regulation.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Physiology

Background:

  • Gap junctions (GJs) mediate direct cell-to-cell communication and adhesion, crucial for tissue function.
  • Precise regulation of GJs is essential, yet their renewal and cell separation present challenges due to stable channel structures.
  • Previous understanding of GJ degradation involved proteasomal and endo-/lysosomal pathways.

Purpose of the Study:

  • To investigate the degradation pathway of internalized gap junctions (GJs).
  • To elucidate the molecular mechanisms governing GJ turnover.
  • To identify novel pathways involved in connexin 43 (Cx43) degradation.

Main Methods:

  • Utilized fluorescently tagged connexin 43 (Cx43-GFP/YFP/mApple) in HeLa cells.
  • Performed ultrastructural analyses and confocal colocalization microscopy.
  • Employed pharmacological treatments and RNAi to deplete key autophagic proteins and assess p62 involvement.

Main Results:

  • Demonstrated that internalized GJs are degraded through autophagy.
  • Identified the ubiquitin-binding protein p62/sequestosome 1 as a key factor in targeting internalized GJs to autophagic degradation.
  • Provided evidence for an alternative GJ degradation pathway distinct from previously known proteasomal and endo-/lysosomal routes.

Conclusions:

  • Gap junctions are degraded via autophagy, mediated by the p62 protein.
  • This study uncovers a novel autophagic degradation pathway for GJs.
  • Understanding this pathway is important for cellular communication regulation and has implications for health and disease.