Role of signal transduction pathway of mitogen-activated protein kinase on metastasis of hepatocellular carcinoma induced by VEGF

2001 ◽  
Vol 2 (1) ◽  
pp. 38-41
Author(s):  
Mao Hua ◽  
Yuan Aili ◽  
Zhao Minfang ◽  
Lai Zuosheng
1993 ◽  
Vol 13 (9) ◽  
pp. 5659-5669 ◽  
Author(s):  
M Tyers ◽  
B Futcher

In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.


2005 ◽  
Vol 57 (6) ◽  
pp. 617-623 ◽  
Author(s):  
Jeff L. Browning ◽  
Tushar Patel ◽  
Paul C. Brandt ◽  
Keith A. Young ◽  
Leigh A. Holcomb ◽  
...  

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