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Phosphorylation-Dependent Differences in CXCR4-LASP1-AKT1 Interaction between Breast Cancer and Chronic Myeloid Leukemia

Institute of Experimental Biomedicine, University Hospital Wuerzburg, Josef-Schneider-Straße 2, 97080 Wuerzburg, Germany
Institute of Molecular Cell Biology, CMB-Center for Molecular Biomedicine, University Hospital Jena, Hans-Knöll-Straße 2, 07745 Jena, Germany
Rudolf Virchow Center for Experimental Biomedicine, University of Wuerzburg, Josef-Schneider-Str. 5, 97080 Wuerzburg, Germany
Institute for Cardiovascular Prevention, LMU Munich, 80336 Munich, Germany
Cardiovascular Research Institute Maastricht, Department of Biochemistry, Maastricht University, 6229 ER Maastricht, The Netherlands
DZHK (German Centre for Cardiovascular Research), partner site Munich Heart Alliance, 80802 Munich, Germany
Klinik für Innere Medizin II, Abteilung für Hämatologie und internistische Onkologie, Universitätsklinikum Jena, Am Klinikum 1, 07747 Jena, Germany
Author to whom correspondence should be addressed.
Cells 2020, 9(2), 444; (registering DOI)
Received: 3 December 2019 / Revised: 4 February 2020 / Accepted: 11 February 2020 / Published: 14 February 2020
The serine/threonine protein kinase AKT1 is a downstream target of the chemokine receptor 4 (CXCR4), and both proteins play a central role in the modulation of diverse cellular processes, including proliferation and cell survival. While in chronic myeloid leukemia (CML) the CXCR4 is downregulated, thereby promoting the mobilization of progenitor cells into blood, the receptor is highly expressed in breast cancer cells, favoring the migratory capacity of these cells. Recently, the LIM and SH3 domain protein 1 (LASP1) has been described as a novel CXCR4 binding partner and as a promoter of the PI3K/AKT pathway. In this study, we uncovered a direct binding of LASP1, phosphorylated at S146, to both CXCR4 and AKT1, as shown by immunoprecipitation assays, pull-down experiments, and immunohistochemistry data. In contrast, phosphorylation of LASP1 at Y171 abrogated these interactions, suggesting that both LASP1 phospho-forms interact. Finally, findings demonstrating different phosphorylation patterns of LASP1 in breast cancer and chronic myeloid leukemia may have implications for CXCR4 function and tyrosine kinase inhibitor treatment. View Full-Text
Keywords: LASP1; CXCR4; AKT1; CML; breast cancer LASP1; CXCR4; AKT1; CML; breast cancer
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Butt, E.; Stempfle, K.; Lister, L.; Wolf, F.; Kraft, M.; Herrmann, A.B.; Viciano, C.P.; Weber, C.; Hochhaus, A.; Ernst, T.; Hoffmann, C.; Zernecke, A.; Frietsch, J.J. Phosphorylation-Dependent Differences in CXCR4-LASP1-AKT1 Interaction between Breast Cancer and Chronic Myeloid Leukemia. Cells 2020, 9, 444.

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