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Your search keyword '"Scherer, Steven S"' showing total 14 results
Start Over Author "Scherer, Steven S" Journal journal of neuroscience research
14 results on '"Scherer, Steven S"'

14. Cx29 and Cx32, two connexins expressed by myelinating glia, do not interact and are functionally distinct.

Author

Ahn M, Lee J, Gustafsson A, Enriquez A, Lancaster E, Sul JY, Haydon PG, Paul DL, Huang Y, Abrams CK, and Scherer SS

Subjects
Animals, COS Cells, Cell Differentiation genetics, Cell Membrane metabolism, Cell Membrane ultrastructure, Chlorocebus aethiops, Connexins chemistry, Connexins genetics, Gap Junctions metabolism, Gap Junctions ultrastructure, HeLa Cells, Humans, Mice, Mutant Chimeric Proteins chemistry, Mutant Chimeric Proteins genetics, Mutant Chimeric Proteins metabolism, Myelin Sheath ultrastructure, Nerve Tissue Proteins chemistry, Nerve Tissue Proteins genetics, Nervous System ultrastructure, Neuroglia ultrastructure, Protein Structure, Tertiary physiology, Gap Junction beta-1 Protein, Connexins metabolism, Myelin Sheath metabolism, Nerve Tissue Proteins metabolism, Nervous System growth & development, Nervous System metabolism, Neuroglia metabolism
Abstract

In rodents, oligodendrocytes and myelinating Schwann cells express connexin32 (Cx32) and Cx29, which have different localizations in the two cell types. We show here that, in contrast to Cx32, Cx29 does not form gap junction plaques or functional gap junctions in transfected cells. Furthermore, when expressed together, Cx29 and Cx32 are not colocalized and do not coimmunoprecipitate. To determine the structural basis of their divergent behavior, we generated a series of chimeric Cx32-Cx29 proteins by exchanging their intracellular loops and/or their C-terminal cytoplasmic tails. Although some chimerae reach the cell membrane, others appear to be largely localized intracellularly; none form gap junction plaques or functional gap junctions. Substituting the C-terminus or the intracellular loop and the C-terminus of Cx32 with those of Cx29 does not disrupt their colocalization or coimmunoprecipitation with Cx32. Substituting the C-terminus of Cx29 with that of Cx32 does not disrupt the coimmunoprecipitation or the colocalization with Cx29, whereas substituting both the intracellular loop and the C-terminus of Cx32 with those of Cx29 diminishes the coimmunoprecipitation with Cx29. Conversely, the Cx32 chimera that contains the intracellular loop of Cx29 coimmunoprecipitates with Cx29, indicating that the intracellular loop participates in Cx29-Cx29 interactions. These data indicate that homomeric interactions of Cx29 and especially Cx32 largely require other domains: the N-terminus, transmembrane domains, and extracellular loops. Substituting the intracellular loop and/or tail of Cx32 with those of Cx29 appears to prevent Cx32 from forming functional gap junctions.

Published
2008
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