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The lyn tyrosine kinase is essential for erythropoietin induced erythroid differentiation and specifically interacts with lckbp-1/hs1 and several novel molecules

Ingley, E., Tilbrook, P.A., Williams, J.H., Hibbs, M.L., Tsai, S. and Klinken, S.P. (1997) The lyn tyrosine kinase is essential for erythropoietin induced erythroid differentiation and specifically interacts with lckbp-1/hs1 and several novel molecules. FASEB Journal, 11 (9).

Abstract

Erythropoietin (EPO) stimulates the immature erythroid J2E cell line to terminally di.fferentiate, proliferate and maintains their viability in the absence of serum. In contrast, a mutant J2E clone (J2E-NR) fails to mature in response to the hormone which we have shown is due to a very low expression level of the Lyn tyrosine kinase. Co-immunoprecipitation and yeast two-hybrid analysis indicates that Lyn directly associates with the EPO-receptor complex. Using the yeast two hybrid system we have identified LckBP-1/HS1 and several novel molecules as Lyn interactors. LckBP-1/HS1 has been shown to bind to the SH3 domain of Lck and contains four tandem helix-turn-helix motifs, a proline rich region, a proline and glutamine rich segment, and an SH3 domain. The importance of this interaction in EPO-induced signalling through Lyn is currently be!ng investigated. Three novel molecules were also identified in the two-hybrid screen as specifically interacting with Lyn. One of these has an ankyrin repeat most closely related to a K+ channel. Another novel protein bound specifically to a kinase inactive mutant of Lyn where tyrosine 397 had been mutated to phenyalanine. Full-length clones of these novel molecules are currently being isolated and their involvement in erythroid development will be analysed.

Publication Type: Journal Article
Publisher: FASEB
URI: http://researchrepository.murdoch.edu.au/id/eprint/39585
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