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First published online May 21, 2007

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Toxic clues to cadherin processing

Enterotoxigenic strains of Bacteroides fragilis can cause serious health problems, in part because they secrete the metalloprotease toxin BFT. This induces degradation of E-cadherin cell-adhesion molecules in intestinal epithelial cells (IECs), disassembly of the adherens junctions between cells, and release of the E-cadherin-associated transcription factor -catenin, which stimulates cell proliferation. Now, on p. 1868, Cynthia Sears and co-workers reveal that BFT-induced cleavage of E-cadherin in IECs involves multiple steps and depends on the toxin's own proteolytic activity and -secretase, an endogenous intramembrane protease that processes Notch and the amyloid precursor APP. The authors show first that BFT promotes shedding of the ectodomain of E-cadherin. Whether this effect is direct or indirect is unclear but, report the authors, it is not mediated by host cell proteases that release the E-cadherin ectodomain in other cell lines. After the E-cadherin ectodomain has been shed, -secretase processes the intracellular E-cadherin domain and releases a distinct pool of -catenin. From this and other results, the authors conclude that at least two differentially regulated pools of -catenin associate with E-cadherin and that the one regulated by -secretase controls IEC homeostasis.

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JCS 2007 120: 1868-1876. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content