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A more recent version of this article appeared on June 1, 2002
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Submitted on November 29, 2001
Revised on March 8, 2002
Accepted on March 20, 2002
1 Instituto de Microbiología Bioquímica and Centro de Investigación del Cáncer, Consejo Superior de Investigaciones Científicas-Universidad de Salamanca, Spain
* Corresponding author. E-mail address: atanasio{at}usal.es.
The ectodomain of certain transmembrane proteins can be released by the action of cell surface proteases, termed secretases. Here we have investigated how mitogen-activated protein kinases (MAPKs) control the shedding of membrane proteins. We show that Erk acts as an intermediate in PKC-regulated TrkA cleavage. We report that the cytosolic tail of the Tumor necrosis factor 
-Converting Enzyme (TACE) is phosphorylated by Erk at Threonine 735. In addition, we show that Erk and TACE associate. This association is favoured by Erk activation, and by the presence of Threonine 735. In contrast to the Erk route, the p38 MAPK was able to stimulate TrkA cleavage in cells devoid of TACE activity, indicating that other proteases are also involved in TrkA shedding. These results demonstrate that secretases are able to discriminate between the different stimuli that trigger membrane protein ectodomain cleavage, and indicate that phosphorylation by MAPKs may regulate the proteolytic function of membrane secretases.
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