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@article{andre_situ_2009,
title = {In situ chemical cross-linking on living cells reveals {CD9P}-1 cis-oligomer at cell surface},
volume = {73},
issn = {1876-7737},
url = {http://dx.doi.org/10.1016/j.jprot.2009.08.005},
doi = {10.1016/j.jprot.2009.08.005},
abstract = {Tetraspanins are integral membrane proteins involved in a variety of physiological and pathological processes. They associate with each other in multimolecular complexes containing numerous membrane proteins. As a first step towards the study of the supramolecular organization of tetraspanin complexes, we have implemented a proteomic approach based on in situ protein cross-linking on living cells followed by affinity purification of tetraspanin complexes. This allowed observing the presence of high molecular weight protein complexes that were characterized as containing CD9P-1/CD315 using LC-MS/MS. Western blot analyses and the use of different tags demonstrated the presence of CD9P-1 oligomer in cis-association at cell surface. A significant amount of CD9P-1 oligomer was observed on various cell types. We have shown that CD9P-1 self-associates independently from its association with tetraspanins. However, the expression level of CD9 or CD81 that associate directly and specifically with CD9P-1, positively modulates the cross-linking efficiency of CD9P-1. Thus, tetraspanins can play a role on CD9P-1 oligomerization status.},
number = {1},
journal = {J Proteomics},
author = {André, Magali and Chambrion, Célia and Charrin, Stéphanie and Soave, Sabrina and Chaker, Joëlle and Boucheix, Claude and Rubinstein, Eric and Le Naour, François},
year = {2009},
pages = {93--102},
}