Abstract by Pramoda Aththota Gamage

Personal Infomation

Presenter's Name

Pramoda Aththota Gamage

Degree Level



Tsz-Yin Chan
Chrissy Egbert
Kristina Kohler
Maddie Frey
Julia Maxson
David Huang
Steven Warner
David Bearss
Jeffrey Tyner

Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Joshua Andersen


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.