RNA-Binding Protein HuR Regulates Both Mutant and Wild-Type IDH1 in IDH1-Mutated Cancer

The Norris lab recently identified two RNA binding proteins required for proper neuron-specific splicing. The lab conducted touch- response behavioral assays to assess the function of these proteins in touch-sensing neurons. After isolating C. elegans worms with specific phenotypes, the lab used automated computer tracking and video analysis to record the worms’ behavior. The behavior of mutant worms differed from that of wild-type worms. The Norris lab also discovered two possible RNA binding protein sites in SAD-1, a neuronal gene implicated in the neuronal development of C. elegans1. These two binding sites may control the splicing of SAD-1. The lab transferred mutated DNA into the genome of wild-type worms by injecting a mutated plasmid. The newly transformed worms fluoresced green, indicating that the two binding sites control SAD-1 splicing.

Download Full-text

The wild type RNase L but not mutant laboratory and natural variants suppresses the RNA binding protein, HUR: Effects on cytokine 3′ UTR

Cytokine ◽

10.1016/j.cyto.2009.07.142 ◽

2009 ◽

Vol 48 (1-2) ◽

pp. 50

Author(s):

Latifa Al-Haj ◽

Wijdan Al-Ahamdi ◽

Maha Al-Ghamdi ◽

Maher Al-Saif ◽

Edward Hitti ◽

...

Keyword(s):

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Rnase L ◽

Wild Type ◽

Natural Variants

Download Full-text

Mice Deficient for Testis-Brain RNA-Binding Protein Exhibit a Coordinate Loss of TRAX, Reduced Fertility, Altered Gene Expression in the Brain, and Behavioral Changes

Molecular and Cellular Biology ◽

10.1128/mcb.23.18.6419-6434.2003 ◽

2003 ◽

Vol 23 (18) ◽

pp. 6419-6434 ◽

Cited By ~ 69

Author(s):

Vargheese Chennathukuzhi ◽

Joel M. Stein ◽

Ted Abel ◽

Stacy Donlon ◽

Shicheng Yang ◽

...

Keyword(s):

Gene Expression ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Mitotic Cell ◽

Seminiferous Tubules ◽

Factor X ◽

Wild Type ◽

Altered Gene Expression ◽

Altered Gene

ABSTRACT Testis-brain RNA-binding protein (TB-RBP), the mouse orthologue of the human protein Translin, is a widely expressed and highly conserved protein with proposed functions in chromosomal translocations, mitotic cell division, and mRNA transport and storage. To better define the biological roles of TB-RBP, we generated mice lacking TB-RBP. Matings between heterozygotes gave rise to viable, apparently normal homozygous mutant mice at a normal Mendelian ratio. The TB-RBP-related and -interacting protein Translin-associated factor X was reduced to 50% normal levels in heterozygotes and was absent in TB-RBP-null animals. The null mice were 10 to 30% smaller than their wild-type or heterozygote littermates at birth and remained so to about 6 to 9 months of age, showed normal B- and T-cell development, and accumulated visceral fat. TB-RBP-null male mice were fertile and sired offspring but had abnormal seminiferous tubules and reduced sperm counts. Null female mice were subfertile and had reduced litter sizes. Microarray analysis of total brain RNA from null and wild-type mice revealed an altered gene expression profile with the up-regulation of 14 genes and the down-regulation of 217 genes out of 12,473 probe sets. Numerous neurotransmitter receptors and ion channels, including γ-aminobutyric acid A receptor α1 and glutamate receptor α3, were strongly down-regulated. Behavioral abnormalities were also seen. Compared to littermates, the TB-RBP-null mice appeared docile and exhibited reduced Rota-Rod performance.

Download Full-text

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy

Brain ◽

10.1093/brain/awz313 ◽

2019 ◽

Vol 142 (12) ◽

pp. 3753-3770 ◽

Cited By ~ 10

Author(s):

Han-Jou Chen ◽

Simon D Topp ◽

Ho Sang Hui ◽

Elsa Zacco ◽

Malvika Katarya ◽

...

Keyword(s):

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Wild Type ◽

Inclusion Formation

TDP-43 is a DNA/RNA binding protein, but whether its interactions with RNA are relevant to inclusion formation in ALS is unclear. Chen et al. report that mutated forms of TDP-43 that are unable to bind RNA have an increased tendency to aggregate, and can mediate toxicity by sequestering wild-type TDP-43.

Download Full-text

The plastid-nucleus located DNA/RNA binding protein WHIRLY1 regulates microRNA-levels during stress

10.1101/197202 ◽

2017 ◽

Cited By ~ 2

Author(s):

Aleksandra Swida-Barteczka ◽

Anja Krieger-Liszkay ◽

Wolfgang Bilger ◽

Ulrike Voigt ◽

Götz Hensel ◽

...

Keyword(s):

Transgenic Plants ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Nuclear Gene ◽

Retrograde Signaling ◽

Wild Type ◽

Transcriptional Responses ◽

Stress Dependent

In this article a novel mechanism of retrograde signaling by chloroplasts during stress is described. This mechanism involves the DNA/RNA binding protein WHIRLY1 as a regulator of microRNA levels. By virtue of its dual localization in chloroplasts and the nucleus of the same cell, WHIRLY1 was proposed as an excellent candidate coordinator of chloroplast function and nuclear gene expression (Grabowski et al., 2008; Foyer et al., 2014). In this study the putative involvement of WHIRLY1 in stress dependent retrograde signaling was investigated by comparison of barley (Hordeum vulgare L., cv. Golden Promise) wild-type and transgenic plants with an RNAi-mediated knockdown of WHIRLY1. In contrast to the wild type, the transgenic plants were unable to cope with continuous high light conditions. They were impaired in production of several microRNAs mediating post-transcriptional responses during stress (Kruszka et al., 2012, Sunkar et al., 2012). The results support a central role of WHIRLY1 in retrograde signaling and underpin a so far underestimated role of microRNAs in this process.

Download Full-text