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Blood, 16 April 2009, Vol. 113, No. 16, pp. 3845-3856. Prepublished online as a Blood First Edition Paper on December 8, 2008; DOI 10.1182/blood-2008-04-153452. This Article Full Text (PDF) Supplemental Tables, Figures, and Video All Versions of this Article: blood-2008-04-153452v1 113/16/3845    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Samuels, A. L Articles by Ingley, E. Search for Related Content PubMed PubMed Citation Articles by Samuels, A. L Articles by Ingley, E. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted April 25, 2008 Accepted December 2, 2008 Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation Amy L Samuels, S. Peter Klinken, and Evan Ingley* Cell Signaling Group, WA Institute for Medical Research and Centre for Medical Research, The University of Western Australia, Perth, WA, Australia Laboratory for Cancer Medicine, WA Institute for Medical Research and Centre for Medical Research, The University of Western Australia, Perth, WA, Australia * Corresponding author; email: eingley{at}waimr.uwa.edu.au. Erythropoiesis is primarily controlled by erythropoietin (Epo), which stimulates proliferation, differentiation and survival of erythroid precursors. We have previously shown that the tyrosine kinase Lyn is critical for transducing differentiation signals emanating from the activated Epo receptor. A yeast two-hybrid screen for downstream effectors of Lyn identified a novel protein, Liar (Lyn interacting ankyrin repeat), which forms a multi-protein complex with Lyn and HS1 in erythroid cells. Interestingly, three of the ankyrin repeats of Liar define a novel SH3 binding region for Lyn and HS1. Liar also contains functional nuclear localisation and nuclear export sequences, and shuttles rapidly between the nucleus and cytoplasm. Ectopic expression of Liar inhibited the differentiation of normal erythroid progenitors, as well as immortalised erythroid cells. Significantly, Liar affected Epo-activated signaling molecules including Erk2, STAT5, Akt and Lyn. These results show that Liar is a novel Lyn-interacting molecule that plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Truth or dare: role of Liar in EPO-dependent signaling Dwayne L. Barber Blood 2009 113: 3650-3651. [Full Text] [PDF] This article has been cited by other articles: D. L. Barber Truth or dare: role of Liar in EPO-dependent signaling Blood, April 16, 2009; 113(16): 3650 - 3651. [Full Text] [PDF]

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