scholarly journals Moderate and strong static magnetic fields directly affect EGFR kinase domain orientation to inhibit cancer cell proliferation

Oncotarget ◽  
2016 ◽  
Vol 7 (27) ◽  
pp. 41527-41539 ◽  
Author(s):  
Lei Zhang ◽  
Jihao Wang ◽  
HongLei Wang ◽  
Wenchao Wang ◽  
Zhiyuan Li ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Magnetic Fields ◽  
Cancer Cell ◽  
Kinase Domain ◽  
Cancer Cell Proliferation ◽  
Static Magnetic Fields ◽  
Domain Orientation ◽  
Egfr Kinase

scholarly journals SUMOylation Is Required for ERK5 Nuclear Translocation and ERK5-Mediated Cancer Cell Proliferation

2020 ◽  
Vol 21 (6) ◽  
pp. 2203 ◽  
Author(s):  
Tatiana Erazo ◽  
Sergio Espinosa-Gil ◽  
Nora Diéguez-Martínez ◽  
Néstor Gómez ◽  
Jose M Lizcano
Keyword(s):  
Cell Proliferation ◽  
Cancer Cell ◽  
Nuclear Localization ◽  
Transcriptional Activation ◽  
Molecular Mechanisms ◽  
Nuclear Translocation ◽  
Kinase Domain ◽  
Cancer Cell Proliferation ◽  
Transcriptional Activation Domain ◽  
Nuclear Shuttling

The MAP kinase ERK5 contains an N-terminal kinase domain and a unique C-terminal tail including a nuclear localization signal and a transcriptional activation domain. ERK5 is activated in response to growth factors and stresses and regulates transcription at the nucleus by either phosphorylation or interaction with transcription factors. MEK5-ERK5 pathway plays an important role regulating cancer cell proliferation and survival. Therefore, it is important to define the precise molecular mechanisms implicated in ERK5 nucleo-cytoplasmic shuttling. We previously described that the molecular chaperone Hsp90 stabilizes and anchors ERK5 at the cytosol and that ERK5 nuclear shuttling requires Hsp90 dissociation. Here, we show that MEK5 or overexpression of Cdc37—mechanisms that increase nuclear ERK5—induced ERK5 Small Ubiquitin-related Modifier (SUMO)-2 modification at residues Lys6/Lys22 in cancer cells. Furthermore, mutation of these SUMO sites abolished the ability of ERK5 to translocate to the nucleus and to promote prostatic cancer PC-3 cell proliferation. We also show that overexpression of the SUMO protease SENP2 completely abolished endogenous ERK5 nuclear localization in response to epidermal growth factor (EGF) stimulation. These results allow us to propose a more precise mechanism: in response to MEK5 activation, ERK5 SUMOylation favors the dissociation of Hsp90 from the complex, allowing ERK5 nuclear shuttling and activation of the transcription.

scholarly journals SUMOylation is Required for ERK5 Nuclear Translocation and ERK5-Mediated Cancer Cell Proliferation

2020 ◽  
Author(s):  
Tatiana Erazo ◽  
Sergio Espinosa-Gil ◽  
Nora Diéguez-Martínez ◽  
Néstor Gómez ◽  
Jose M. Lizcano
Keyword(s):  
Cell Proliferation ◽  
Cancer Cell ◽  
Nuclear Localization ◽  
Transcriptional Activation ◽  
Molecular Mechanisms ◽  
Nuclear Translocation ◽  
Kinase Domain ◽  
Cancer Cell Proliferation ◽  
Transcriptional Activation Domain ◽  
Nuclear Shuttling

The MAP kinase ERK5 contains an N-terminal kinase domain and a unique C-terminal tail including a nuclear localization signal and a transcriptional activation domain. ERK5 is activated in response to growth factors and stresses, and regulates transcription at the nucleus by either phosphorylation or interaction with transcription factors. MEK5-ERK5 pathway plays an important role regulating cancer cell proliferation and survival. Therefore, it is important to define the precise molecular mechanisms implicated in ERK5 nucleo-cytoplasmic shuttling. We previously described that the molecular chaperone Hsp90 stabilizes and anchors ERK5 at the cytosol, and that ERK5 nuclear shuttling requires Hsp90 dissociation. Here, we show that MEK5 or Cdc37 overexpression -mechanisms that induce nuclear ERK5- induced ERK5 SUMO-2 modification at residues Lys6/Lys22 in cancer cells. We also show that overexpression of the SUMO protease SENP2 completely abolished endogenous ERK5 nuclear localization in response to EGF stimulation. Furthermore, mutation of these SUMO sites abolished the ability of ERK5 to translocate to the nucleus and to promote prostatic cancer PC-3 cell proliferation. These results allow us to propose a more precise mechanism: in response to MEK5 activation, ERK5 SUMOylation favors the dissociation of Hsp90 from the complex, allowing ERK5 nuclear shuttling and activation of transcription.

NF-κB regulates colon cancer cell proliferation and tumorigenicity

2001 ◽  
Vol 120 (5) ◽  
pp. A615-A615
Author(s):  
S KUWADA ◽  
C SCAIFE ◽  
J KUANG ◽  
R DAYNES
Keyword(s):  
Colon Cancer ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Colon Cancer Cell ◽  
Cancer Cell Proliferation

Compounds inhibiting hyperglycemia and cancer cell proliferation from Morus alba L

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
S Sun ◽  
M Zhang ◽  
M Li ◽  
F Guan ◽  
F Wu ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cancer Cell ◽  
Morus Alba ◽  
Cancer Cell Proliferation

Exendin-4, a Glucagon-Like Peptide-1 Receptor Agonist, Attenuates Prostate Cancer Cell Proliferation via Phosphorylation of MKP-1

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 1957-P
Author(s):  
TAKAKO KAWANAMI ◽  
TAKASHI NOMIYAMA ◽  
YURIKO HAMAGUCHI ◽  
TOMOKO TANAKA ◽  
TOSHIHIKO YANASE
Keyword(s):  
Prostate Cancer ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Receptor Agonist ◽  
Prostate Cancer Cell ◽  
Cancer Cell Proliferation ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1
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