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J Biol Chem, Vol. 275, Issue 19, 14608-14614, May 12, 2000
From the Departments of Many membrane-bound proteins, including
cytokines, receptors, and growth factors, are proteolytically cleaved
to release a soluble form of their extracellular domain. The tumor
necrosis factor (TNF)-
Functional Analysis of the Domain Structure of Tumor Necrosis
Factor-
Converting Enzyme*
§,,
,,
Cell Sciences,
¶ Biochemistry, Molecular Biology, ** Molecular Immunology,
and Research Administration, Immunex
Corporation, Seattle, Washington 98101
converting enzyme (TACE/ADAM-17) is a
transmembrane metalloproteinase responsible for the proteolytic release
or "shedding" of several cell-surface proteins, including TNF and
p75 TNFR. We established a TACE-reconstitution system using
TACE-deficient cells co-transfected with TACE and substrate cDNAs
to study TACE function and regulation. Using the TACE-reconstitution
system, we identified two additional substrates of TACE, interleukin
(IL)-1R-II and p55 TNFR. Using truncations and chimeric constructs of
TACE and another ADAM family member, ADAM-10, we studied the function of the different domains of TACE in three shedding activities. We found
that TACE must be expressed with its membrane-anchoring domain for
phorbol ester-stimulated shedding of TNF, p75 TNFR, and IL-1R-II, but
that the cytoplasmic domain is not required for the shedding of these
substrates. The catalytic domain of ADAM-10 could not be functionally
substituted for that of TACE. IL-1R-II shedding required the
cysteine-rich domain of TACE as well as the catalytic domain, whereas
TNF and p75 TNFR shedding required only the tethered TACE catalytic domain.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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M. X. G. |
