English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The claudin megatrachea protein complex.

MPS-Authors
/persons/resource/persons32558

Jaspers,  M.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15649

Plessmann,  U.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons41374

Nikolov,  M.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15806

Schuh,  R.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

1570048.pdf
(Publisher version), 4MB

Supplementary Material (public)

1570048_jbc.M112.399410-1.xls
(Supplementary material), 97KB

1570048_jbc.M112.399410-2.pdf
(Supplementary material), 43KB

1570048_jbc.M112.399410-3.xls
(Supplementary material), 3MB

1570048_jbc.M112.399410-4.pdf
(Supplementary material), 39KB

1570048_jbc.M112.399410-6.pdf
(Supplementary material), 393KB

1570048_jbc.M112.399410-5.pdf
(Supplementary material), 107KB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-260D-E
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.