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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. |
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Keywords:cell biology, SHIP2, MLK3, JIP1 |
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