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  The claudin megatrachea protein complex.

Jaspers, M., Nolde, K., Behr, M., Joo, S. H., Plessmann, U., Nikolov, M., et al. (2012). The claudin megatrachea protein complex. Journal of Biological Chemistry, 287(44), 36756-36765. doi:10.1074/jbc.M112.399410.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-260D-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CF5D-D
Genre: Journal Article

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 Creators:
Jaspers, M.1, Author              
Nolde, K., Author
Behr, M., Author
Joo, S. H., Author
Plessmann, U.2, Author              
Nikolov, M.2, Author              
Urlaub, H.2, Author              
Schuh, R.1, Author              
Affiliations:
1Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society, ou_578591              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Claudins are integral transmembrane components of the tight junctions forming trans-epithelial barriers in many organs, such as the nervous system, lung, and epidermis. In Drosophila three claudins have been identified that are required for forming the tight junctions analogous structure, the septate junctions (SJs). The lack of claudins results in a disruption of SJ integrity leading to a breakdown of the trans-epithelial barrier and to disturbed epithelial morphogenesis. However, little is known about claudin partners for transport mechanisms and membrane organization. Here we present a comprehensive analysis of the claudin proteome in Drosophila by combining biochemical and physiological approaches. Using specific antibodies against the claudin Megatrachea for immunoprecipitation and mass spectrometry, we identified 142 proteins associated with Megatrachea in embryos. The Megatrachea interacting proteins were analyzed in vivo by tissue-specific knockdown of the corresponding genes using RNA interference. We identified known and novel putative SJ components, such as the gene product of CG3921. Furthermore, our data suggest that the control of secretion processes specific to SJs and dependent on Sec61p may involve Megatrachea interaction with Sec61 subunits. Also, our findings suggest that clathrin-coated vesicles may regulate Megatrachea turnover at the plasma membrane similar to human claudins. As claudins are conserved both in structure and function, our findings offer novel candidate proteins involved in the claudin interactome of vertebrates and invertebrates.

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Language(s): eng - English
 Dates: 2012-10-26
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M112.399410
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 287 (44) Sequence Number: - Start / End Page: 36756 - 36765 Identifier: -