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SHIP2 interacts with MLK3 and regulates its tyrosine phosphorylation
WU Zhe 1,XIE Jingwei 2 * #
1.Department of Neurology, first Affiliated hospital, China Medical University, Shenyang, 110001
2.Department of pathophysiology, China Medical University, Shenyang, 110122
*Correspondence author
#Submitted by
Subject:
Funding: Specialized Research Fund for the Doctoral Program of Higher Education(No.20112104120010), Special financial grant from the China postdoctoral Science foundation (No.201104615), National Natural Science Funds of China (No.Grant No.81141070), Liaoning science and technology project (No.201225021)
Opened online:16 November 2015
Accepted by: none
Citation: WU Zhe,XIE Jingwei.SHIP2 interacts with MLK3 and regulates its tyrosine phosphorylation[OL]. [16 November 2015] http://en.paper.edu.cn/en_releasepaper/content/4660744
 
 
MLK3, a serine/threonine MAP3K, implicates in various physiological functions as neurodegenerative disease, cell cycle regulation, apoptosis and T-cell activation etc. Phosphorylation of MLK3 is essential for its activation. Ocassionally, in our previous study, MLK3 was found to be phosphorylated at tyrosine site which had not reported yet. Data in the present study show that SHIP2 positively regulated MLK3 tyrosine phosphorylation through SHIP2-MLK3 interaction, and JIP1 showed negative effect on this tyrosine phosphorylation. In addition, SHIP2-MLK3 association was not modulated in response to EGF or TNF-α. Domain tests demonstrate that the catalytic domain of SHIP2 was responsible for the interaction with MLK3. All together, our data may provide a new potential regulating mechaniam of cross-talk between SHIP2 and MLK3-mediated MAPK pathway.
Keywords:cell biology, SHIP2, MLK3, JIP1
 
 
 

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