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Published 28 October 2002. doi:10.1083/jcb.200207050
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© The Rockefeller University Press, 0021-9525/2002/10/361 $5.00
The Journal of Cell Biology, Volume 159, Number 2, 361-372

Article

Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells



Sebastian Poliak1, Sean Matlis1, Christoph Ullmer2, Steven S. Scherer3 and Elior Peles1

1 Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel
2 Biofrontera Pharmaceuticals GmbH, Hemmelratherweg 201, D-51377 Leverkusen, Germany
3 Department of Neurology, The University of Pennsylvania Medical Center, Philadelphia, PA 19104

Address correspondence to Dr. Elior Peles, Dept. of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: 972-8-934-2941. Fax: 972-8-934-4195. E-mail: peles{at}weizmann.ac.il

The apposed membranes of myelinating Schwann cells are joined by several types of junctional specializations known as autotypic or reflexive junctions. These include tight, gap, and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman, and mesaxons. The molecular components of autotypic tight junctions have not been established. Here we report that two homologues of Discs Lost–multi PDZ domain protein (MUPP)1, and Pals-associated tight junction protein (PATJ), are differentially localized in myelinating Schwann cells and associated with different claudins. PATJ is mainly found at the paranodal loops, where it colocalized with claudin-1. MUPP1 and claudin-5 colocalized in the incisures, and the COOH-terminal region of claudin-5 interacts with MUPP1 in a PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner. In developing nerves, claudin-5 and MUPP1 appear together in incisures during the first postnatal week, suggesting that they coassemble during myelination. Finally, we show that the incisures also contain four other PDZ proteins that are found in epithelial tight junctions, including three membrane-associated guanylate-kinase proteins (membrane-associated guanylate-kinase inverted-2, ZO-1, and ZO-2) and the adaptor protein Par-3. The presence of these different tight junction proteins in regions of noncompact myelin may be required to maintain the intricate cytoarchitecture of myelinating Schwann cells.

Key Words: tight junction; MUPP1; PATJ; Schmidt-Lanterman incisures; paranodal loops


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