scholarly journals FRAXE-associated mental retardation protein (FMR2) is an RNA-binding protein with high affinity for G-quartet RNA forming structure

2009 ◽  
Vol 37 (4) ◽  
pp. 1269-1279 ◽  
Author(s):  
Mounia Bensaid ◽  
Mireille Melko ◽  
Elias G. Bechara ◽  
Laetitia Davidovic ◽  
Antonio Berretta ◽  
...  
Neuroscience ◽  
2017 ◽  
Vol 349 ◽  
pp. 64-75 ◽  
Author(s):  
Lin-Tao Zhou ◽  
Shun-Hua Ye ◽  
Hai-Xuan Yang ◽  
Yong-Ting Zhou ◽  
Qi-Hua Zhao ◽  
...  

Glia ◽  
2019 ◽  
Vol 68 (3) ◽  
pp. 495-508 ◽  
Author(s):  
Caleb A. Doll ◽  
Katie M. Yergert ◽  
Bruce H. Appel

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39338 ◽  
Author(s):  
Rachid El Fatimy ◽  
Sandra Tremblay ◽  
Alain Y. Dury ◽  
Samuel Solomon ◽  
Paul De Koninck ◽  
...  

2006 ◽  
Vol 15 (9) ◽  
pp. 1525-1538 ◽  
Author(s):  
Laetitia Davidovic ◽  
Elias Bechara ◽  
Maud Gravel ◽  
Xavier H. Jaglin ◽  
Sandra Tremblay ◽  
...  

2017 ◽  
Vol 292 (39) ◽  
pp. 16221-16234 ◽  
Author(s):  
Lingna Yang ◽  
Chongyuan Wang ◽  
Fudong Li ◽  
Jiahai Zhang ◽  
Anam Nayab ◽  
...  

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.


2020 ◽  
Vol 218 (3) ◽  
Author(s):  
Alexander Saveliev ◽  
Sarah E. Bell ◽  
Martin Turner

Cell migration relies on coordinated activity of chemotactic and guidance receptors. Here, we report a specific role for the RNA-binding protein ZFP36L1 in limiting the abundance of molecules involved in the homing of antibody-secreting cells (ASCs) to the bone marrow (BM). In the absence of ZFP36L1, ASCs build up in the spleen and the liver and show diminished accumulation in the BM. ZFP36L1 facilitates migration by directly regulating G protein–coupled receptor kinase 2 (GRK2) and the integrin chains α4 and β1 in splenic ASCs. Expression of CXCR4 and of the integrins α4 and β1 is differentially regulated on ASCs produced at the early and late stages of the immune response. Consequently, deletion of the Zfp36l1 gene has a stronger effect on BM accumulation of high-affinity ASCs formed late in the response. Thus, ZFP36L1 is an integral part of the regulatory network controlling gene expression during ASC homing.


Author(s):  
Claudia Bagni ◽  
Eric Klann

Chapter 8 discusses how Fragile X syndrome (FXS) is caused by the absence of the RNA-binding protein fragile X mental retardation protein (FMRP). FMRP is highly expressed in the brain and gonads, the two organs mainly affected in patients with the syndrome. Functionally, FMRP belongs to the family of RNA-binding proteins, shuttling from the nucleus to the cytoplasm, and, as shown for other RNA-binding proteins, forms large messenger ribonucleoparticles.


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