T. Schmidt et al., A novel protein (Fbf-1) that binds to CD95/APO-1/FAS and shows sequence similarity to trichohyalin and plectin, BBA-GENE ST, 1493(1-2), 2000, pp. 249-254
Citations number
16
Categorie Soggetti
Molecular Biology & Genetics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
The Fas/Apo-1/CD95 cell surface receptor belongs to the TNF receptor family
of cell death inducing molecules. A number of cytosolic adapter proteins t
hat mediate signal transduction of CD95 have been characterized, but some f
eatures of the molecular mechanisms of CD95-induced cell death remain elusi
ve. We describe here a novel protein that can interact with the cytosolic d
omain of the murine CD95 receptor in a yeast two-hybrid assay. This novel p
rotein was termed Fbf-1 for Fas binding factor and bears no sequence simila
rity to the known CD95 adapter proteins. Fbf-1 is 1173 aa long and has a th
eoretical. molecular weight of around 130 kDa. The protein is expressed in
a wide variety of tissues and is localized in the cytoplasm, Fbf-1 is a ver
y hydrophilic protein, highly conserved between mouse and human and bears a
carboxyterminal leucine heptad repeat reminiscent of leucine zipper protei
n interaction domains, In addition, it shows sequence similarity to trichoh
yalin and plectin pointing to a function as a structural protein. (C) 2000
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