TY  - JOUR
A1  - Butt, Elke
A1  - Stempfle, Katrin
A1  - Lister, Lorenz
A1  - Wolf, Felix
A1  - Kraft, Marcella
A1  - Herrmann, Andreas B.
A1  - Viciano, Cristina Perpina
A1  - Weber, Christian
A1  - Hochhaus, Andreas
A1  - Ernst, Thomas
A1  - Hoffmann, Carsten
A1  - Zernecke, Alma
A1  - Frietsch, Jochen J.
T1  - Phosphorylation-dependent differences in CXCR4-LASP1-AKT1 interaction between breast cancer and chronic myeloid leukemia
T2  - Cells
N2  - 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.
KW  - LASP1
KW  - CXCR4
KW  - AKT1
KW  - CML
KW  - breast cancer
Y1  - 2020
UR  - https://opus.bibliothek.uni-wuerzburg.de/frontdoor/index/index/docId/20063
UR  - https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-200638
SN  - 2073-4409
VL  - 9
IS  - 2
ER  -