Adherens junctions in myelinating Schwann cells stabilize Schmidt-Lanterman incisures via recruitment of p120 catenin to E-cadherin Journal Article
| Authors: | Tricaud, N.; Perrin-Tricaud, C.; Bruses, J. L.; Rutishauser, U. |
| Article Title: | Adherens junctions in myelinating Schwann cells stabilize Schmidt-Lanterman incisures via recruitment of p120 catenin to E-cadherin |
| Abstract: | Schwann cell myelin contains highly compacted layers of membrane as well as noncompacted regions with a visible cytoplasm. One of these cytoplasmic compartments is the Schmidt-Lanterman incisure, which spirals through the compacted layers and is believed to help sustain the growth and function of compact myelin. Incisures contain adherens junctions (AJs), the key components of which are E-cadherin, its cytoplasmic partners called catenins, and F-actin. To explore in vivo the role of cadherin and catenins in incisures, E-cadherin mutant proteins that completely replace endogenous cadherin have been delivered to the cells using adenovirus. When the introduced cadherin lacked its extracellular domain, association of p120 catenin (p120ctn) with the cadherin did not occur, and incisures disappeared. Remarkably, the additional replacement of two phosphorylatable tyrosines by phenylalanine in the cytoplasmic tail of the mutant cadherin restored both p120ctn binding and incisure architecture, indicating that p120ctn recruitment is critical for incisures maintenance and might be regulated by phosphorylations. In addition, the ability of the p 120ctn/cadherin complex to support incisures was blocked by mutation of the Rho GTPase regulatory region of the p 120ctn, and downregulation of Rac1 activity at the junction reversed this inhibition. Because Rho GTPases regulate the state of the actin filaments, these findings suggest that one role of p120ctn in incisures is to organize the cytoskeleton at the AJ. Finally, developmental studies of Schwann cells demonstrated that p120ctn recruitment from the cytoplasm to the AJ occurs before the appearance of Rac1 GTPase and F-actin at the junction. Copyright © 2005 Society for Neuroscience. |
| Keywords: | immunohistochemistry; controlled study; protein phosphorylation; dna-binding proteins; nonhuman; animal cell; mouse; animals; mice; mice, knockout; animal tissue; cell compartmentalization; nerve tissue proteins; protein binding; morphogenesis; in vivo study; age factors; diagnostic imaging; transfection; tyrosine; phosphorylation; uvomorulin; cloning, molecular; blotting, western; regulatory mechanism; immunoprecipitation; phosphoproteins; cytoplasm; green fluorescent proteins; cell adhesion molecules; cell count; protein structure, tertiary; down regulation; schwann cell; animals, newborn; cell junction; beta catenin; cadherins; mutagenesis; rho guanine nucleotide binding protein; rho gtp-binding proteins; axons; extracellular space; myelination; phenylalanine; adenoviridae; adherens junctions; cho cells; cricetinae; cricetulus; microscopy, electron, transmission; schwann cells; sciatic nerve; cytoarchitecture; actin filament; myelin sheath; 2',3'-cyclic-nucleotide phosphodiesterases; rac1 gtp-binding protein; catenin; protein p120; connexins; adherens junction; p120 catenin; schmidt lanterman incisure; ranvier's nodes |
| Journal Title: | The Journal of Neuroscience |
| Volume: | 25 |
| Issue: | 13 |
| ISSN: | 0270-6474 |
| Publisher: | Society for Neuroscience |
| Date Published: | 2005-03-30 |
| Start Page: | 3259 |
| End Page: | 3269 |
| Language: | English |
| DOI: | 10.1523/jneurosci.5168-04.2005 |
| PUBMED: | 15800180 |
| PROVIDER: | scopus |
| PMCID: | PMC6724905 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 26" - "Export Date: 24 October 2012" - "CODEN: JNRSD" - "Source: Scopus" |
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