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J Biol Chem, Vol. 274, Issue 53, 38241-38250, December 31, 1999
From the The CD95 death receptor plays an important role
in several physiological and pathological apoptotic processes involving
in particular the immune system. CD95 ligation leads to clustering of
the receptor cytoplasmic "death domains" and recruitment of the
zymogen form of caspase-8 to the cell surface. Activation of this
protease through self-cleavage, followed by activation of downstream
effector caspases, culminates in cleavage of a set of cellular proteins
resulting in apoptosis with disassembly of the cell. It is very well
known that the extracellular region of the CD95 receptor is required
for CD95L interaction and that the death domain is necessary for the
induction of the apoptotic signaling. Here, we identified and
characterized a novel CD95 ligand- and death domain-independent
oligomerization domain mapping to the NH2-terminal
extracellular region of the CD95 receptor. In vitro and
in vivo studies indicated that this domain, conserved among
all soluble CD95 variants, mediates homo-oligomerization of the CD95
receptor and of the soluble CD95 proteins, as well as
hetero-oligomerization of the receptor with the soluble variants. These
results offer new insight into the mechanism of apoptosis inhibition
mediated by the soluble CD95 proteins and suggest a role of the
extracellular oligomerization domain in the regulation of the
non-signaling state of the CD95 receptor.
Identification and Characterization of a Ligand-independent
Oligomerization Domain in the Extracellular Region of the CD95
Death Receptor*
§,,,,
Institute of Cell Biology, National Research
Council, Campus "Adriano Buzzati-Traverso," Via E. Ramarini 32,
00016 Monterotondo Scalo, Rome and ¶ Nu.M.E.D. Group, Clinica
Medica II, University "La Sapienza," 00161 Rome, Italy
*
This work was supported in part by grants from the Italian
Association for Cancer Research, by European Community Contracts CHRX-CT94-0537 and BMH4-CT96-0300, and by Italian National Institute of
Health AIDS Program Grant 9403-98.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.
To whom correspondence should be addressed. Tel.:
39-06-90091263; Fax: 39-06-90091260; E-mail:
gruberti@ibc.rm.cnr.it.
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