Abstract
ZNF198 is fused with FGFR1 in an atypical myeloproliferative disease that results in constitutive activation of the kinase domain and mislocalization to the cytoplasm. We have used immunoprecipitation of a GFP-tagged ZNF198 combined with MALDI-TOF mass spectroscopy to identify interacting proteins. P splicing factor (PSF) was identified as one of the proteins and this interaction was confirmed by Western blotting. Other proteins identified were the spliceosomal components hnRNP A2/B1, hnRNP H3, and TLS/FUS. PSF is also known to interact with PTB, another member of the hnRNP family of proteins, and we further demonstrated that PTB interacts with ZNF198. The interaction between TLS/FUS and ZNF198 was confirmed using Western blot analysis. In 293 cells expressing the ZNF198/FGFR1 fusion protein, neither PSF nor PTB binds to the fusion protein, possibly because of their differential localization in the cell.
Original language | English (US) |
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Pages (from-to) | 78-85 |
Number of pages | 8 |
Journal | Experimental Cell Research |
Volume | 309 |
Issue number | 1 |
DOIs | |
State | Published - Sep 10 2005 |
Externally published | Yes |
Keywords
- Leukemia
- Mass spectroscopy
- RNA maturation
- RNA upstream binding factor
- TLS
- ZNF198/FGFR1
ASJC Scopus subject areas
- Cell Biology