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J Biol Chem, Vol. 274, Issue 38, 26978-26984, September 17, 1999
-Chain mRNA Results in a Shortened Form with a Distinct
Pattern of Expression
From the Groupe de Recherche Cytokines et
Récepteurs, Unité INSERM 463, Institut de Biologie, 9 Quai
Moncousu, 44035 Nantes Cedex 01, France
We report the existence of eight different
interleukin-15 receptor 
-chain (IL-15R) transcripts resulting
from exon-splicing mechanisms within the IL-15R gene. Two main
classes of transcripts can be distinguished that do or do not (
2
isoforms) contain the exon 2-coding sequence. Both classes were
expressed in numerous cell lines and tissues (including peripheral
blood lymphocytes) at comparable levels and could be transcribed in
COS-7 cells, and the proteins were expressed at the cell surface. Both
receptor forms displayed numerous glycosylation states, reflecting
differential usage of a single N-glycosylation site as well
as extensive O-glycosylations. Whereas IL-15R bound
IL-15 with high affinity, 2IL-15R was unable to bind IL-15, thus
revealing the indispensable role of the exon 2-encoded domain in
cytokine binding. A large proportion of IL-15R was expressed at the
nuclear membrane with some intranuclear localization, supporting a
potential direct action of the IL-15·IL-15R complex at the nuclear
level. In sharp contrast, 2IL-15R was found only in the
non-nuclear membrane compartments, indicating that the exon 2-encoded
domain (which is shown to contain a potential nuclear localization
signal) plays an important role in receptor post-translational routing.
Together, our data indicate that exon 2 splicing of human IL-15R is
a natural process that might play regulatory roles at different levels.
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