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Localization of phosphorylated connexin 43 using serial section immunogold electron microscopy.

Rachael P Norris1, Valentina Baena2, Mark Terasaki1

  • 1Department of Cell Biology, University of Connecticut Health Center, Farmington, CT 06030, USA Norris@uchc.edu terasaki@uchc.edu.

Journal of Cell Science
|February 17, 2017
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Summary
This summary is machine-generated.

Connexosomes, formed during gap junction turnover, are double membrane-enclosed vesicles. Phosphorylation of connexin 43 at S262 indicates a role in connexosome formation, crucial for gap junction internalization.

Keywords:
Annular gap junctionsConnexinConnexosomesImmunogoldPhosphorylationSerial section electron microscopy

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Gap junction turnover involves the formation of connexosomes, double membrane-enclosed vesicles derived from gap junction plaques.
  • Phosphorylation is a key regulatory mechanism in gap junction dynamics, but precise protein associations require further investigation.
  • Distinguishing between gap junctions and connexosomes, and identifying their associated proteins, is essential for understanding gap junction turnover.

Purpose of the Study:

  • To investigate the formation and protein composition of connexosomes using advanced electron microscopy techniques.
  • To determine the phosphorylation status of connexin 43 (GJA1) in gap junctions and connexosomes.
  • To elucidate the role of specific connexin 43 phosphorylation sites in gap junction internalization and connexosome processing.

Main Methods:

  • Utilized serial section electron microscopy with automated tape collecting ultramicrotome (ATUM) for high-resolution imaging of mouse ovarian follicles.
  • Employed immunolabeling techniques on serial sections to identify and localize specific phosphorylated residues of connexin 43.
  • Analyzed the three-dimensional organization of gap junctions and connexosomes within their native cellular environment.

Main Results:

  • Connexosomes were observed to form from various cellular structures, including adjacent cell bodies, thin cell processes, and the same cell.
  • Phosphorylation of connexin 43 at serine residue S368 was detected in both gap junctions and connexosomes.
  • Phosphorylation of connexin 43 at serine residue S262 was specifically found on a subset of connexosomes, suggesting a role in their formation or processing.

Conclusions:

  • Phosphorylation at S262 of connexin 43 is implicated in connexosome formation or subsequent processing.
  • These findings provide precise evidence that phosphorylation plays a critical role in the internalization of gap junctions.
  • Serial section electron microscopy of immunogold-labeled tissues is a powerful method for studying the 3D organization of cellular structures.