scholarly journals Enod40, a Short Open Reading Frame–Containing mRNA, Induces Cytoplasmic Localization of a Nuclear RNA Binding Protein in Medicago truncatula

2004 ◽  
Vol 16 (4) ◽  
pp. 1047-1059 ◽  
Author(s):  
Anna Campalans ◽  
Adam Kondorosi ◽  
Martin Crespi
1995 ◽  
Vol 182 (3) ◽  
pp. 865-874 ◽  
Author(s):  
Q Tian ◽  
J Taupin ◽  
S Elledge ◽  
M Robertson ◽  
P Anderson

We have identified a serine/threonine kinase that is rapidly activated during Fas-mediated apoptosis. Fas-activated serine/threonine kinase (FAST) is phosphorylated on serine and threonine residues in Jurkat cells. In response to Fas ligation, it is rapidly dephosphorylated and concomitantly activated to phosphorylate TIA-1, a nuclear RNA-binding protein that has been implicated as an effector of apoptosis. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation, suggesting a role in signaling downstream events in the apoptotic program. Our results introduce Fast and TIA-1 as components of a molecular cascade involved in signaling Fas-mediated apoptosis.


2005 ◽  
Vol 25 (18) ◽  
pp. 8139-8149 ◽  
Author(s):  
Yong Zhong Xu ◽  
Sergio Di Marco ◽  
Imed Gallouzi ◽  
Marek Rola-Pleszczynski ◽  
Danuta Radzioch

ABSTRACT The solute carrier family 11 member 1 (SLC11A1, formerly NRAMP1) gene is associated with infectious and autoimmune diseases and plays an important role in macrophage activation. Human SLC11A1 mRNA contains an AU-rich element (ARE) within the 3′ untranslated region; however, its role in the regulation of SLC11A1 gene expression has not been elucidated. Here we analyze the expression of SLC11A1 in human monocytes and HL-60 cells and then use HL-60 cells as a model to determine whether RNA-binding protein HuR is associated with the ARE and involved in SLC11A1 mRNA turnover. Our results demonstrate a binding of HuR to the SLC11A1 ARE in phorbol myristate acetate (PMA)-differentiated cells dramatically increased compared to that in undifferentiated cells. Interestingly, PMA-induced accumulation of cytoplasmic HuR occurs in parallel with an increase in the binding of HuR to SLC11A1 ARE and with an increase in the SLC11A1 mRNA level. This suggests that HuR's cytoplasmic localization plays an important role in the regulation of SLC11A1 expression. We also observe that down-regulation of HuR expression by RNA interference (RNAi) results in a decrease in SLC11A1 expression which can be restored by the addition of recombinant HuR protein to the RNAi-treated cells. Finally, we show that HuR overexpression in HL-60 cells significantly increases the SLC11A1 mRNA stability. Taken together, our data demonstrate that HuR is a key mediator of posttranscriptional regulation and expression of the SLC11A1 gene.


1997 ◽  
Vol 17 (6) ◽  
pp. 3194-3201 ◽  
Author(s):  
R J Buckanovich ◽  
R B Darnell

Nova-1, an autoantigen in paraneoplastic opsoclonus myoclonus ataxia (POMA), a disorder associated with breast cancer and motor dysfunction, is a neuron-specific nuclear RNA binding protein. We have identified in vivo Nova-1 RNA ligands by combining affinity-elution-based RNA selection with protein-RNA immunoprecipitation. Starting with a pool of approximately 10(15) random 52-mer RNAs, we identified long stem-loop RNA ligands that bind to Nova-1 with high affinity (Kd of approximately 2 nM). The loop region of these RNAs harbors a approximately 15-bp pyrimidine-rich element [UCAU(N)(0-2)]3 which is essential for Nova-1 binding. Mutagenesis studies defined the third KH domain of Nova-1 and the [UCAU(N)(0-2)]3 element as necessary for in vitro binding. Consensus [UCAU (N)(0-2)], elements were identified in two neuronal pre-mRNAs, one encoding the inhibitory glycine receptor alpha2 (GlyR alpha2) and a second encoding Nova-1 itself. Nova-1 protein binds these RNAs with high affinity and specificity in vitro, and this binding can be blocked by POMA antisera. Moreover, both Nova-1 and GlyR alpha2 pre-mRNAs specifically coimmunoprecipitated with Nova-1 protein from brain extracts. Thus, Nova-1 functions as a sequence-specific nuclear RNA binding protein in vivo; disruption of the specific interaction between Nova-1 and GlyR alpha2 pre-mRNA may underlie the motor dysfunction seen in POMA.


2017 ◽  
Vol 212 ◽  
pp. 16-20 ◽  
Author(s):  
Olivera Cirovic ◽  
Roman Trikin ◽  
Anneliese Hoffmann ◽  
Nicholas Doiron ◽  
Martin Jakob ◽  
...  

2008 ◽  
Vol 17 (18) ◽  
pp. 2803-2818 ◽  
Author(s):  
Ingrid Ehrmann ◽  
Caroline Dalgliesh ◽  
Aikaterini Tsaousi ◽  
Maria Paola Paronetto ◽  
Bettina Heinrich ◽  
...  

2018 ◽  
Vol 66 (2) ◽  
pp. 244-253 ◽  
Author(s):  
Helisa H. Wippel ◽  
Juliane S. Malgarin ◽  
Sharon de Toledo Martins ◽  
Newton M. Vidal ◽  
Bruna H. Marcon ◽  
...  

2011 ◽  
Vol 6 ◽  
pp. 10 ◽  
Author(s):  
Anne Kristin Aksaas ◽  
Anja C V Larsen ◽  
Marie Rogne ◽  
Ken Rosendal ◽  
Anne-Katrine Kvissel ◽  
...  

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