Abstract by Pramoda Aththota Gamage
Pramoda Aththota Gamage
Chemistry and Biochemistry
Oncogenic capacity of TNK1 clinical mutants control the 14-3-3 binding
Non-receptor tyrosine kinase 1 (TNK1) is poorly characterized. In previous studies TNK1 has been identified as an oncogenic kinase in multiple genome-wide screening but its function and regulation in cancer is largely unknown. Our Previous data suggest an interaction between TNK1 and 14-3-3 which is an oncogenic phospho binding protein and also a cluster of phosphorylation within the proline-rich domain of TNK1 that regulates its interaction with 14-3-3. The disruption of 14-3-3 interaction will activate TNK1 kinase activity. We have recently identified several clinical mutants of TNK1 in which 14-3-3 binding are disrupted by truncation. The aim of our current study is to test the oncogenic capacity of these TNK1 clinical mutants in Ba/F3 cell system. We expect that these TNK 1 clinical mutants will disrupt 14-3-3 binding and activate TNK 1 oncogenic kinase activity causing tumorigenesis.