scholarly journals RNA‐binding protein PUM2 regulates mesenchymal stem cell fate via repression of JAK2 and RUNX2 mRNAs

2019 ◽  
Vol 235 (4) ◽  
pp. 3874-3885 ◽  
Author(s):  
Myon‐Hee Lee ◽  
Xinjun Wu ◽  
Yong Zhu
Keyword(s):  
Stem Cell ◽  
Mesenchymal Stem Cell ◽  
Cell Fate ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stem Cell Fate

scholarly journals Targeted mRNA Decay by RNA Binding Protein AUF1 Regulates Adult Muscle Stem Cell Fate, Promoting Skeletal Muscle Integrity

Cell Reports ◽  
2016 ◽  
Vol 16 (5) ◽  
pp. 1379-1390 ◽  
Author(s):  
Devon M. Chenette ◽  
Adam B. Cadwallader ◽  
Tiffany L. Antwine ◽  
Lauren C. Larkin ◽  
Jinhua Wang ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Stem Cell ◽  
Cell Fate ◽  
Mrna Decay ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Muscle Stem Cell ◽  
Stem Cell Fate ◽  
Adult Muscle

scholarly journals Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs

2019 ◽  
Vol 48 (4) ◽  
pp. 1843-1871 ◽  
Author(s):  
René M Arvola ◽  
Chung-Te Chang ◽  
Joseph P Buytendorp ◽  
Yevgen Levdansky ◽  
Eugene Valkov ◽  
...  
Keyword(s):  
Stem Cell ◽  
Catalytic Activity ◽  
Protein Expression ◽  
Cell Fate ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Stem Cell Fate ◽  
Target Mrnas ◽  
N Terminus ◽  
Decapping Enzyme

Abstract Pumilio is an RNA-binding protein that represses a network of mRNAs to control embryogenesis, stem cell fate, fertility and neurological functions in Drosophila. We sought to identify the mechanism of Pumilio-mediated repression and find that it accelerates degradation of target mRNAs, mediated by three N-terminal Repression Domains (RDs), which are unique to Pumilio orthologs. We show that the repressive activities of the Pumilio RDs depend on specific subunits of the Ccr4–Not (CNOT) deadenylase complex. Depletion of Pop2, Not1, Not2, or Not3 subunits alleviates Pumilio RD-mediated repression of protein expression and mRNA decay, whereas depletion of other CNOT components had little or no effect. Moreover, the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further, we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme, Dcp2, participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs. Because the N-terminal RDs are conserved in mammalian Pumilio orthologs, the results of this work broadly enhance our understanding of Pumilio function and roles in diseases including cancer, neurodegeneration and epilepsy.

scholarly journals Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs

2019 ◽  
Author(s):  
René M. Arvola ◽  
Chung-Te Chang ◽  
Joseph P. Buytendorp ◽  
Yevgen Levdansky ◽  
Eugene Valkov ◽  
...  
Keyword(s):  
Stem Cell ◽  
Catalytic Activity ◽  
Protein Expression ◽  
Cell Fate ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Stem Cell Fate ◽  
Target Mrnas ◽  
N Terminus ◽  
Decapping Enzyme

ABSTRACTPumilio is an RNA-binding protein that represses a network of mRNAs to control embryogenesis, stem cell fate, fertility, and neurological functions in Drosophila. We sought to identify the mechanism of Pumilio-mediated repression and find that it accelerates degradation of target mRNAs, mediated by three N-terminal Repression Domains (RDs), which are unique to Pumilio orthologs. We show that the repressive activities of the Pumilio RDs depend on specific subunits of the Ccr4-Not (CNOT) deadenylase complex. Depletion of Pop2, Not1, Not2, or Not3 subunits alleviates Pumilio RD-mediated repression of protein expression and mRNA decay, whereas depletion of other CNOT components had little or no effect. Moreover, the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further, we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme, Dcp2, participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs. Because the N-terminal RDs are conserved in mammalian Pumilio orthologs, the results of this work broadly enhance our understanding of Pumilio function and roles in diseases including cancer, neurodegeneration, and epilepsy.

Regulation of the mesenchymal stem cell fate by interleukin-17: Implications in osteogenic differentiation

2021 ◽  
Vol 13 (11) ◽  
pp. 1699-1716
Author(s):  
Jelena Krstić ◽  
Slavko Mojsilović ◽  
Sonja S Mojsilović ◽  
Juan F Santibanez
Keyword(s):  
Stem Cell ◽  
Mesenchymal Stem Cell ◽  
Osteogenic Differentiation ◽  
Cell Fate ◽  
Interleukin 17 ◽  
Stem Cell Fate

The effects of poly(dimethylsiloxane) surface silanization on the mesenchymal stem cell fate

2015 ◽  
Vol 3 (2) ◽  
pp. 383-390 ◽  
Author(s):  
Yon Jin Chuah ◽  
Shreyas Kuddannaya ◽  
Min Hui Adeline Lee ◽  
Yilei Zhang ◽  
Yuejun Kang
Keyword(s):  
Cell Culture ◽  
Stem Cell ◽  
Mesenchymal Stem Cell ◽  
Cell Fate ◽  
Stem Cell Fate

Surface silanization with 3-aminopropyl triethoxy silane (APTES) ± glutaraldehyde (GA) enhanced the biocompatibility of poly(dimethylsiloxane) surfaces for long term cell culture investigation.

scholarly journals Effects of magnesium degradation products on mesenchymal stem cell fate and osteoblastogenesis

Gene ◽  
2016 ◽  
Vol 575 (1) ◽  
pp. 9-20 ◽  
Author(s):  
Bérengère J.C. Luthringer ◽  
Regine Willumeit-Römer
Keyword(s):  
Stem Cell ◽  
Mesenchymal Stem Cell ◽  
Cell Fate ◽  
Degradation Products ◽  
Stem Cell Fate

scholarly journals The RNA‐binding protein Imp2 regulates oxidative phosporylation that is key to glioblastoma cancer stem cell maintenance

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Michalina Janiszewska ◽  
Mario-Luca Suva ◽  
Riekelt H. Houtkooper ◽  
Virginie Clement-Schatlo ◽  
Ivan Stamenkovic
Keyword(s):  
Stem Cell ◽  
Cancer Stem Cell ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stem Cell Maintenance ◽  
Cell Maintenance
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