Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Jhun, B.H. et al.

The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit.

We have cloned a protein tyrosine kinase, MATK, which is expressed abundantly in megakaryocytes and the brain. We investigated whether MATK participates in the c-Kit ligand/stem cell factor (KL/ SCF) signaling pathway in the megakaryocytic cell line CMK. After KL/ SCF stimulation, five major proteins of molecular masses of 145, 113, 92, 76, and 63 kDa were rapidly and transiently tyrosine-phosphorylated in a time-dependent manner, peaking within 5 min, and returning to basal levels within 60 min. To study the role of MATK in the KL/ SCF signaling pathway, glutathione S-transferase ( GST) fusion proteins containing SH2 and SH3 domains of MATK were cloned, expressed in Escherichia coli, and purified. MATK-SH2, but not MATK-SH3, precipitated the tyrosine-phosphorylated c-Kit (molecular mass of 145 kDa) in KL/ SCF- stimulated CMK cells. Other GST fusion proteins containing the SH2 domain of p85 of phosphatidylinositol 3-kinase, phospholipase C gamma-1, and ras-GAP also precipitated c-Kit. The tyrosine-phosphorylated c-Kit was co-immunoprecipitated with anti-MATK and anti-p85 antibodies in KL/ SCF- stimulated CMK cells, but not in granulocyte-macrophage colony stimulating factor or interleukin-6-stimulated cells, suggesting receptor specificity. These results indicate that MATK associates with the c-Kit receptor following specific stimulation by KL/ SCF via its SH2 domain and likely participates in transduction of growth signals induced by this cytokine in megakaryocytes.[1]

References

The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit. Jhun, B.H., Rivnay, B., Price, D., Avraham, H. J. Biol. Chem. (1995) [Pubmed]

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