The histone demethylase KDM2B activates FAK and PI3K that control tumor cell motility
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The histone demethylase KDM2B activates FAK and PI3K that control tumor cell motility. / Zacharopoulou, Nefeli; Kallergi, Galatea; Alkahtani, Saad; Tsapara, Anna; Alarifi, Saud; Schmid, Evi; Sukkar, Basma; Kampranis, Sotirios; Lang, Florian; Stournaras, Christos.
In: Cancer Biology and Therapy, Vol. 21, No. 6, 2020, p. 533-540.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The histone demethylase KDM2B activates FAK and PI3K that control tumor cell motility
AU - Zacharopoulou, Nefeli
AU - Kallergi, Galatea
AU - Alkahtani, Saad
AU - Tsapara, Anna
AU - Alarifi, Saud
AU - Schmid, Evi
AU - Sukkar, Basma
AU - Kampranis, Sotirios
AU - Lang, Florian
AU - Stournaras, Christos
PY - 2020
Y1 - 2020
N2 - Recent studies revealed that the histone demethylase KDM2B regulates the epithelial markers E-Cadherin and ZO-1, the RhoA/B/C-small-GTPases and actin cytoskeleton organization, in DU-145 prostate- and HCT-116 colon-tumor cells. Here we addressed the role of KDM2B in the activation of Focal Adhesion Kinase (FAK)-signaling and its involvement in regulating tumor cell motility. We used RT-PCR for gene transcriptional analysis, Western blotting for the assessment of protein expression and activity and wound-healing assay for the study of cell migration. KDM2B overexpression or silencing controls the activity of FAK in DU-145 prostate- and HCT-116 colon-tumor cells without affecting gene transcription and protein expression of this kinase. Upon KDM2B overexpression in DU-145 cells, significantly enhanced migration was observed, which was abolished in cells pretreated by the specific phosphoinositide-3 kinase (PI3 K) inhibitor LY294002, implying involvement of FAK/PI3 K signaling in the migration process. In line with this, the p85-PI3 K-subunit was downregulated upon knockdown of KDM2B in DU-145 cells, while the opposite effect became evident in KDM2B-overexpressing cells. These results revealed a novel functional role of KDM2B in regulating the activation of the FAK/PI3 K signaling in prostate cancer cells that participates in the control of cell motility.
AB - Recent studies revealed that the histone demethylase KDM2B regulates the epithelial markers E-Cadherin and ZO-1, the RhoA/B/C-small-GTPases and actin cytoskeleton organization, in DU-145 prostate- and HCT-116 colon-tumor cells. Here we addressed the role of KDM2B in the activation of Focal Adhesion Kinase (FAK)-signaling and its involvement in regulating tumor cell motility. We used RT-PCR for gene transcriptional analysis, Western blotting for the assessment of protein expression and activity and wound-healing assay for the study of cell migration. KDM2B overexpression or silencing controls the activity of FAK in DU-145 prostate- and HCT-116 colon-tumor cells without affecting gene transcription and protein expression of this kinase. Upon KDM2B overexpression in DU-145 cells, significantly enhanced migration was observed, which was abolished in cells pretreated by the specific phosphoinositide-3 kinase (PI3 K) inhibitor LY294002, implying involvement of FAK/PI3 K signaling in the migration process. In line with this, the p85-PI3 K-subunit was downregulated upon knockdown of KDM2B in DU-145 cells, while the opposite effect became evident in KDM2B-overexpressing cells. These results revealed a novel functional role of KDM2B in regulating the activation of the FAK/PI3 K signaling in prostate cancer cells that participates in the control of cell motility.
KW - FAK
KW - KDM2B
KW - migration
KW - PI3K
KW - prostate cancer
U2 - 10.1080/15384047.2020.1736481
DO - 10.1080/15384047.2020.1736481
M3 - Journal article
C2 - 32175798
AN - SCOPUS:85081733791
VL - 21
SP - 533
EP - 540
JO - Cancer Biology & Therapy
JF - Cancer Biology & Therapy
SN - 1538-4047
IS - 6
ER -
ID: 253703741