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 ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
High Affinity ◽  
Mental Retardation Protein

scholarly journals Fragile Mental Retardation Protein Interacts with the RNA-Binding Protein Caprin1 in Neuronal RiboNucleoProtein Complexes

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39338 ◽  
Author(s):  
Rachid El Fatimy ◽  
Sandra Tremblay ◽  
Alain Y. Dury ◽  
Samuel Solomon ◽  
Paul De Koninck ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Ribonucleoprotein Complexes ◽  
Mental Retardation Protein

scholarly journals The human RNA-binding protein and E3 ligase MEX-3C binds the MEX-3–recognition element (MRE) motif with high affinity

2017 ◽  
Vol 292 (39) ◽  
pp. 16221-16234 ◽  
Author(s):  
Lingna Yang ◽  
Chongyuan Wang ◽  
Fudong Li ◽  
Jiahai Zhang ◽  
Anam Nayab ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
E3 Ligase ◽  
Recognition Element ◽  
High Affinity

scholarly journals The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo.

1997 ◽  
Vol 17 (6) ◽  
pp. 3194-3201 ◽  
Author(s):  
R J Buckanovich ◽  
R B Darnell
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Motor Dysfunction ◽  
High Affinity ◽  
Loop Region ◽  
Nuclear Rna ◽  
Rna Ligands

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.

scholarly journals Efficient homing of antibody-secreting cells to the bone marrow requires RNA-binding protein ZFP36L1

2020 ◽  
Vol 218 (3) ◽  
Author(s):  
Alexander Saveliev ◽  
Sarah E. Bell ◽  
Martin Turner
Keyword(s):  
Bone Marrow ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Receptor Kinase ◽  
High Affinity ◽  
Guidance Receptors ◽  
G Protein Coupled ◽  
Late Stages ◽  
Antibody Secreting Cells

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.

Molecular Functions of the Mammalian Fragile X Mental Retardation Protein: Insights Into Mental Retardation and Synaptic Plasticity

2013 ◽  
Author(s):  
Claudia Bagni ◽  
Eric Klann
Keyword(s):  
Mental Retardation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Fragile X ◽  
Rna Binding Protein ◽  
Fragile X Mental Retardation ◽  
The Family ◽  
Mental Retardation Protein ◽  
The Brain

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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