Identification of miR-125b targets involved in acute promyelocytic leukemia cell proliferation

2016 ◽  
Vol 478 (4) ◽  
pp. 1758-1763 ◽  
Author(s):  
Yikai Zhang ◽  
Chengwu Zeng ◽  
Shuai Lu ◽  
Tianyu Qin ◽  
Lijian Yang ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Acute Promyelocytic Leukemia ◽  
Leukemia Cell ◽  
Promyelocytic Leukemia ◽  
Acute Promyelocytic Leukemia Cell

Ruthenium metallodendrimers with anticancer potential in an acute promyelocytic leukemia cell line (HL60)

2017 ◽  
Vol 87 ◽  
pp. 39-47 ◽  
Author(s):  
Sylwia Michlewska ◽  
Maksim Ionov ◽  
Dzmitry Shcharbin ◽  
Marta Maroto-Díaz ◽  
Rafael Gomez Ramirez ◽  
...  
Keyword(s):  
Cell Line ◽  
Acute Promyelocytic Leukemia ◽  
Leukemia Cell ◽  
Promyelocytic Leukemia ◽  
Leukemia Cell Line ◽  
Acute Promyelocytic Leukemia Cell ◽  
Promyelocytic Leukemia Cell Line

Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27Kip1 in the acute promyelocytic leukemia cell line NB4

Blood ◽  
2006 ◽  
Vol 107 (3) ◽  
pp. 1133-1140 ◽  
Author(s):  
Christian Kardinal ◽  
Marc Dangers ◽  
Angelika Kardinal ◽  
Alexandra Koch ◽  
Dominique Tobias Brandt ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Cell Line ◽  
Tyrosine Phosphorylation ◽  
Acute Promyelocytic Leukemia ◽  
Leukemia Cell ◽  
Promyelocytic Leukemia ◽  
Leukemia Cell Line ◽  
Acute Promyelocytic Leukemia Cell ◽  
Promyelocytic Leukemia Cell Line

AbstractWe have investigated the role of tyrosine phosphorylation of the cyclin-dependent kinase (cdk) inhibitor p27Kip1 using the acute promyelocytic leukemia cell line NB4 together with granulocyte colony-stimulating factor (G-CSF). Short-term G-CSF stimulation resulted in a rapid tyrosine dephosphorylation of p27Kip1 accompanied by a change in its binding preferences to cdks. On G-CSF stimulation, p27Kip1 dissociated from cdk4 and associated with cdk2. Binding assays with recombinant p27Kip1 confirmed that tyrosine-phosphorylated p27Kip1 preferentially bound to cdk4, whereas unphosphorylated protein preferentially associated with cdk2. In addition, studies with p27Kip1 point mutations revealed a decisive role of Tyr88 and Tyr89 in binding to cdk4. Furthermore, phosphorylation of Tyr88 and Tyr89 was accompanied by strong nuclear translocation of p27Kip1. Taken together, this report provides the first evidence that tyrosine phosphorylation of p27Kip1 plays a crucial role in binding to cdks and its subcellular localization. Moreover, both effects are mediated by application of G-CSF.

Sign in / Sign up

Export Citation Format

Share Document