Structural and Intermolecular Associations Between Connexin36 and Protein Components of the Adherens
1Department of Physiology and Pathophysiology, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, Canada.
Neuroscience
|June 8, 2018
Summary
Adherens junctions and neuronal gap junctions (composed of connexin36) interact in the central nervous system. Key junctional proteins colocalize, suggesting a complex regulating neuronal communication.
Area of Science:
- Neuroscience
- Cell Biology
- Structural Biology
Background:
- Gap junctions and adherens junctions have known relationships in peripheral tissues.
- Their intimate connections in the central nervous system (CNS) remain less understood.
- Adherens junctions are often found near neuronal gap junctions in the CNS.
Purpose of the Study:
- To investigate the localization of adherens junction proteins relative to connexin36 (Cx36)-containing neuronal gap junctions in the CNS.
- To explore the potential structural and functional interactions between these two types of cell junctions.
Main Methods:
- Immunofluorescence microscopy was used to visualize protein localization.
- The study examined several brain regions, focusing on primary afferent neurons in the mesencephalic trigeminal nucleus (MesV).
- Experiments included comparisons in wild-type and connexin36 null mice.
Main Results:
- Adherens junction proteins (N-cadherin, nectin-1, α-catenin, β-catenin) and associated proteins (zonula occludens-1, AF6/afadin) were found to localize near or overlap with Cx36 gap junctions.
- This colocalization was observed in multiple brain regions.
- Adherens junction components were present even in the absence of Cx36, indicating their maintenance.
Conclusions:
- Results support the concept of a multi-molecular composition of electrical synapses, forming an adherens junction-neuronal gap junction complex.
- This complex suggests potential protein-protein interactions influencing electrical synapse structure and function.
- Intracellular signaling pathways may regulate the assembly, maintenance, and turnover of this complex, impacting neuronal communication dynamics.
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