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Pyk2 and Src Mediate Signaling to CCL18‐Induced Breast Cancer Metastasis
Author(s) -
Li HaiYan,
Cui XiuYing,
Wu Wei,
Yu FengYan,
Yao HeRui,
Liu Qiang,
Song ErWei,
Chen JingQi
Publication year - 2014
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.24697
Subject(s) - proto oncogene tyrosine protein kinase src , metastasis , ccl18 , cancer research , phosphorylation , western blot , microbiology and biotechnology , breast cancer , biology , chemistry , cancer , medicine , receptor , chemokine , biochemistry , gene
Pyk2 and Src phosphorylation is initiated by CCL18, which promotes breast cancer metastasis via its functional G protein‐coupled receptor PITPNM3. However, the function of Pyk2 and Src in CCL18‐induced breast cancer metastasis is poorly understood. Quantitative reverse‐transcription polymerase chain reactions (qRT‐PCRs), Western blot, boyden chamber assay, and adherence assay were performed to delineate the consequences of Pyk2/Src in CCL18‐induced breast cancer cells. Co‐immunoprecipitation and immunofluorescence were performed to analyze the interaction of proteins. Upon the binding of CCL18 to PITPNM3, Pyk2 translocates from the cytoplasm to the plasma membrane to form a stable complex with PITPNM3, subsequently activating Src kinase. Moreover, upon stimulation with CCL18, Pyk2 and Src become essential for integrin alpha5/beta1 clustering‐dependent adherence, migration, and invasion. Pyk2 and Src are important in CCL18‐induced breast cancer metastasis. J. Cell. Biochem. 115: 596–603, 2014. © 2013 Wiley Periodicals, Inc.