The cytoplasmic truncated receptor tyrosine kinase ALK‐ homodimer immortalizes and cooperates with ras in cellular transformation

2001 ◽  
Vol 15 (8) ◽  
pp. 1416-1418 ◽  
Author(s):  
Ingrid Simonitsch ◽  
Doris Polgar ◽  
Maria Hajek ◽  
Peter Duchek ◽  
Barbara Skrzypek ◽  
...  
1999 ◽  
Vol 19 (2) ◽  
pp. 1401-1409 ◽  
Author(s):  
Daniel Besser ◽  
Jacqueline F. Bromberg ◽  
James E. Darnell ◽  
Hidesaburo Hanafusa

ABSTRACT The receptor tyrosine kinase Eyk, a member of the Axl/Tyro3 subfamily, activates the STAT pathway and transforms cells when constitutively activated. Here, we compared the potentials of the intracellular domains of Eyk molecules derived from c-Eyk and v-Eyk to transform rat 3Y1 fibroblasts. The v-Eyk molecule induced higher numbers of transformants in soft agar and stronger activation of Stat3; levels of Stat1 activation by the two Eyk molecules were similar. A mutation in the sequence Y933VPL, present in c-Eyk, to the v-Eyk sequence Y933VPQ led to increased activation of Stat3 and increased transformation efficiency. However, altering another sequence, Y862VNT, present in both Eyk molecules to F862VNT markedly decreased transformation without impairing Stat3 activation. These results indicate that activation of Stat3 enhances transformation efficiency and cooperates with another pathway to induce transformation.


2015 ◽  
Vol 20 (5-6) ◽  
pp. 485-508 ◽  
Author(s):  
Theresa M. LaVallee ◽  
Diego Alvarado ◽  
Andrew J. Garton ◽  
E. Sergio Trombetta ◽  
Richard Gedrich ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document