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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1788-1796
FGFR1 is fused to the centrosome-associated protein
CEP110 in the 8p12 stem cell myeloproliferative disorder with
t(8;9)(p12;q33)
Géraldine Guasch,
Gary J. Mack,
Cornel Popovici,
Nicole Dastugue,
Daniel Birnbaum,
Jérome B. Rattner, and
Marie-Josèphe Pébusque
From the Laboratoire d'Oncologie Moléculaire, Inserm U119,
Institut de Cancérologie et d'Immunologie de Marseille,
Marseille, France; the University of Calgary, Alberta, Canada; the
Laboratoire des Hémopathies, Hôpital de Purpan, Toulouse,
France; and the Laboratoire de Biologie des Tumeurs, Institut
Paoli-Calmettes, Marseille, France
The hallmark of the 8p12 stem cell myeloproliferative disorder (MPD)
is the disruption of the FGFR1 gene, which encodes a tyrosine
kinase receptor for members of the fibroblast growth factor family.
FGFR1 can be fused to at least 3 partner genes at chromosomal
regions 6q27, 9q33, or 13q12. We report here the cloning of the
t(8;9)(p12;q33) and the detection of a novel fusion betweenFGFR1 and the CEP110 gene, which codes for a
novel centrosome-associated protein with a unique cell-cycle
distribution. CEP110 is widely expressed at various levels in
different tissues and is predicted to encode a 994-amino acid
coiled-coil protein with 4 consensus leucine zippers
[L-X(6)-L-X(6)-L-X(6)-L]. Both reciprocal fusion transcripts are
expressed in the patient's cells. The CEP110-FGFR1 fusion protein
encodes an aberrant tyrosine kinase of circa 150-kd, which retains most
of CEP110 with the leucine zipper motifs and the catalytic domain of
FGFR1. Transient expression studies show that the CEP110-FGFR1 protein
has a constitutive kinase activity and is located within the cell cytoplasm.
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