作者: NORIKO YOKOYAMA , W. TODD MILLER
DOI: 10.3892/BR.2014.374
关键词:
摘要: Anaplastic lymphoma kinase (ALK) is a member of the receptor tyrosine superfamily. The ALK gene site frequent mutation and chromosomal rearrangement in various types human cancers. A novel translocation was recently identified colorectal cancer between chromosome 2, open reading frame 44 (C2orf44), unknown function. As first step understanding oncogenic properties this fusion protein, C2orf44 cDNA cloned encoded protein characterized, which designated as WD repeat coiled coil containing (WDCP). C-terminal proline-rich segment WDCP shown to mediate binding Src homology 3 domain family hematopoietic cell (Hck). Co-expression with Hck lead phosphorylation WDCP. Chromatographic fractionation WDCP-containing lysates indicates that exists an oligomer mammalian cells. These results suggest that, context ALK-C2orf44 fusion, imposes oligomeric structure on constitutive activation signaling.