PMID- 10480903
OWN - NLM
STAT- MEDLINE
DCOM- 19991013
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 38
DP  - 1999 Sep 17
TI  - Characterization of FIM-FGFR1, the fusion product of the myeloproliferative
      disorder-associated t(8;13) translocation.
PG  - 26922-30
AB  - The t(8;13) translocation found in a rare type of stem cell myeloproliferative
      disorder generates a constitutively activated tyrosine kinase containing
      N-terminal sequence encoded by the FIM gene linked to the FGFR1 kinase domain.
      Here we have further characterized FIM and FIM-FGFR1 proteins. Firstly, we have
      studied their respective subcellular localization. We show that FIM has nuclear
      and nucleolar localization, whereas FIM-FGFR1 is mainly cytoplasmic. Within the
      nucleolus, FIM colocalizes with the upstream binding factor in interphasic cells,
      indicating that FIM may be involved in the regulation of rRNA transcription. We
      demonstrate that the targetting of FIM to the nucleus depends upon its C-terminal
      region, which is absent in the cytoplasmic FIM-FGFR1 protein. Secondly, we
      demonstrate that FIM-FGFR1 has constitutive dimerization capability mediated by
      the FIM N-terminal sequences. Finally, we show that FIM-FGFR1 promotes survival
      of pro-B Ba/F3 cells after interleukin-3 withdrawal, whereas ligand-activated
      FGFR1 induced not only cell survival but also interleukin-3 independence. Taken
      together, these results indicate that FIM-FGFR1 is activated by dimerization as a
      cytoplasmic kinase and suggest that FIM-FGFR1 partially signals through the FGFR1
      pathways.
FAU - Ollendorff, V
AU  - Ollendorff V
AD  - Laboratoire d'Oncologie Moleculaire, U119 INSERM, Institut de Cancerologie et
      d'Immunologie, 27 Boulevard Lei Roure, 13009 Marseille, France.
FAU - Guasch, G
AU  - Guasch G
FAU - Isnardon, D
AU  - Isnardon D
FAU - Galindo, R
AU  - Galindo R
FAU - Birnbaum, D
AU  - Birnbaum D
FAU - Pebusque, M J
AU  - Pebusque MJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (ZMYM2 protein, human)
RN  - 0 (Zmym2 protein, mouse)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - EC 2.7.10.1 (FGFR1 protein, human)
RN  - EC 2.7.10.1 (Fgfr1 protein, mouse)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1)
SB  - IM
MH  - Animals
MH  - Carrier Proteins/*genetics
MH  - Cells, Cultured
MH  - Chromosome Mapping
MH  - *Chromosomes, Human, Pair 13
MH  - *Chromosomes, Human, Pair 8
MH  - DNA-Binding Proteins/*genetics
MH  - Dimerization
MH  - Fibroblast Growth Factors/genetics/metabolism
MH  - Humans
MH  - Mice
MH  - Myeloproliferative Disorders/*genetics
MH  - Receptor Protein-Tyrosine Kinases/*genetics
MH  - Receptor, Fibroblast Growth Factor, Type 1
MH  - Receptors, Fibroblast Growth Factor/*genetics
MH  - Recombinant Fusion Proteins/genetics
MH  - Transcription Factors
MH  - Transfection
MH  - *Translocation, Genetic
EDAT- 1999/09/10 00:00
MHDA- 1999/09/10 00:01
CRDT- 1999/09/10 00:00
PHST- 1999/09/10 00:00 [pubmed]
PHST- 1999/09/10 00:01 [medline]
PHST- 1999/09/10 00:00 [entrez]
AID - 10.1074/jbc.274.38.26922 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 17;274(38):26922-30. doi: 10.1074/jbc.274.38.26922.