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Related Concept Videos

Gap Junctions01:37

Gap Junctions

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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...
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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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ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Tight Junctions01:29

Tight Junctions

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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...
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Contact-dependent Signaling01:19

Contact-dependent Signaling

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Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...
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Recording Gap Junction Current from Xenopus Oocytes
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In situ structure of a gap junction-stomatin complex.

Nils Rosenkranz1,2, Alexandra N Birtasu2,3, Konstantin Wieland2,3

  • 1Department of Molecular Sciences, Institute of Biophysical Chemistry, Goethe University, Max-von-Laue-Straße 9, 60438 Frankfurt, Germany.

Science Advances
|November 5, 2025
PubMed
Summary
This summary is machine-generated.

Researchers visualized gap junctions (GJs) in vivo, revealing hexagonal arrays and a novel protein cap structure. This cap, likely formed by UNC-1 stomatin, may regulate GJ function in nematodes and beyond.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • Gap junctions (GJs) are vital intercellular channels for cell communication and organ function.
  • Existing structural data primarily comes from purified GJs, lacking in situ context.
  • In vivo, GJs exhibit complex heteromeric formations and protein associations.

Purpose of the Study:

  • To determine the in situ structure and organization of gap junctions in Caenorhabditis elegans.
  • To identify associated proteins and their potential roles in GJ function.

Main Methods:

  • Cryo-electron tomography and subtomogram averaging were employed to analyze C. elegans GJs.
  • AlphaFold3 modeling and molecular dynamics simulations were used to predict protein interactions.
  • Expression of GFP-tagged proteins confirmed structural hypotheses.

Main Results:

  • Hexagonal arrays of GJs with distinct wide and narrow conformations were observed in primary embryonal cells.
  • A novel, cap-like cytosolic protein assembly was identified, enclosing the GJ channel pore.
  • Evidence suggests the cap is formed by UNC-1 stomatin, interacting with UNC-9 innexins.

Conclusions:

  • The study provides the first in situ structural insights into C. elegans gap junctions.
  • The identified UNC-1/stomatin cap represents a potential regulatory mechanism for GJ assembly and function.
  • This finding may have implications for understanding GJ regulation in other organisms.