Fusion of the NH2-terminal domain of the basic helix-loop-helix protein TCF12 to TEC in extraskeletal myxoid chondrosarcoma with translocation t(9;15)(q22;q21)

Citation
H. Sjogren et al., Fusion of the NH2-terminal domain of the basic helix-loop-helix protein TCF12 to TEC in extraskeletal myxoid chondrosarcoma with translocation t(9;15)(q22;q21), CANCER RES, 60(24), 2000, pp. 6832-6835
Citations number
33
Categorie Soggetti
Oncology,"Onconogenesis & Cancer Research
Journal title
CANCER RESEARCH
ISSN journal
00085472 → ACNP
Volume
60
Issue
24
Year of publication
2000
Pages
6832 - 6835
Database
ISI
SICI code
0008-5472(200012)60:24<6832:FOTNDO>2.0.ZU;2-J
Abstract
Extraskeletal myxoid chondrosarcomas (EMCs) are characterized by recurrent t(9;22) or t(9;17) translocations resulting in fusions of the NH2-terminal transactivation domains of EWS or TAF2N to the entire TEC protein. We repor t here an EMC with a novel translocation t(9; 15)(q22;q21) and a third type of TEC-containing fusion gene. The chimeric transcript encodes a protein i n which the first 108 amino acids of the NH2-terminus of the basic helix-lo op-helix (bHLH) protein TCF12 is linked to the entire TEC protein. The tran slocation separates the NH2-terminal domain of TCF12 from the bHLH domain a s well as from a potential leucine zipper domain located immediately downst ream of the breakpoint. These results demonstrate that the NH2-terminal tra nsactivation domains of EWS or TAF2N are not unique in their ability to con vert the TEC protein into an oncogenically active fusion protein, and that they may be replaced by a domain from a bHLH protein that presumably endows the fusion protein with similar functions.