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First published online 26 March 2003
doi: 10.1242/jcs.00415
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Research Article |
INSERM EPI 99-36, Laboratoire d'Hématologie, Faculté de Médecine, 27 Bd Jean Moulin, Marseilles 13385 Cedex 5, France
* Author for correspondence (e-mail: Franck.Peiretti{at}medecine.univ-mrs.fr)
Accepted 6 February 2003
Tumor necrosis factor alpha converting enzyme (TACE) is the
metalloprotease-disintegrin responsible for the ectodomain shedding of several
proteins, including tumor necrosis factor 
. Using the yeast two-hybrid
system, we identified the scaffolding protein synapse associated protein 97
(SAP97) as a binding partner of the cytoplasmic domain of TACE. By deletions
and site-directed mutagenesis, we demonstrated that this interaction involved
the PDZ3 domain of SAP97 and the extreme C-terminal amino-acid sequence of
TACE. This interaction as well as the identification of the specific domains
involved was confirmed in vitro by affinity purification and in mammalian
cells by co-immunoprecipitation and alteration of localization analyzed by
immunofluorescence microscopy. In addition, confocal microscopy showed that
endogenous TACE and SAP97 colocalized in some intracellular areas of COS-7
cells and CACO-2 cells. Furthermore, overexpression of SAP97, unlike that of a
mutant form of SAP97 deleted for its PDZ3 domain, altered the ability of TACE
to release its substrates. Altogether, these results demonstrate an
interaction between TACE and SAP97, which may have a functional implication
for the regulation of TACE shedding activity.
Key words: TACE, SAP97, TNF, PDZ3, Protein interaction
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