scholarly journals 3P222 Synaptic stimulation-dependent local translational regulation by a novel RNA-binding protein RNG105

2004 ◽  
Vol 44 (supplement) ◽  
pp. S245
Author(s):  
N. Shiina ◽  
K. Shinkura ◽  
M. Tokunaga
Keyword(s):  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals Identification and characterization of a 44 kDa protein that binds specifically to the 3′-untranslated region of CYP2a5 mRNA: inducibility, subcellular distribution and possible role in mRNA stabilization

1996 ◽  
Vol 313 (3) ◽  
pp. 1029-1037 ◽  
Author(s):  
Olivier GENESTE ◽  
Françoise RAFFALLI ◽  
Matti A. LANG
Keyword(s):  
Half Life ◽  
Untranslated Region ◽  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Blocking Agent ◽  
Subcellular Fractionation ◽  
Mrna Stabilization ◽  
Nuclear Extracts

Stabilization of mRNA is important in the regulation of CYP2a5 expression but the factors involved in the process are not known [Aida and Negishi (1991) Biochemistry 30, 8041–8045]. In this paper, we describe, for the first time, a protein that binds specifically to the 3′-untranslated region of CYP2a5 mRNA and which is inducible by pyrazole, a compound known to increase the half-life of CYP2a5 mRNA. We also demonstrate that pyrazole treatment causes an elongation of the CYP2a5 mRNA poly(A) tail, and that phenobarbital, which is transcriptional activator of the CYP2a5 gene that does not affect the mRNA half-life, neither induces the RNA-binding protein nor affects the poly(A) tail size. SDS/PAGE of the UV-cross-linked RNA–protein complex demonstrated that the RNA-binding protein has an apparent molecular mass of 44 kDa. The protein-binding site was localized to a 70-nucleotide region between bases 1585 and 1655. Treatment of cytoplasmic extracts with an SH-oxidizing agent, diamide, an SH-blocking agent, N-ethylmaleimide or potato acid phosphatase abolished complex-formation, suggesting that the CYP2a5 mRNA-binding protein is subject to post-translational regulation. Subcellular fractionation showed that the 44 kDa protein is present in polyribosomes and nuclei, and that its apparent induction is much stronger in polyribosomes than in nuclear extracts. We propose that this 44 kDA RNA-binding protein is involved in the stabilization of CYP2a5 mRNA by controlling the length of the poly(A) tail.

scholarly journals Novel insights into global translational regulation through Pumilio family RNA-binding protein Puf3p revealed by ribosomal profiling

2018 ◽  
Vol 65 (1) ◽  
pp. 201-212 ◽  
Author(s):  
Zhe Wang ◽  
Xuepeng Sun ◽  
Josephine Wee ◽  
Xiaoxian Guo ◽  
Zhenglong Gu
Keyword(s):  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals A tail of translational regulation

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Gillian A Gray ◽  
Nicola K Gray
Keyword(s):  
Protein Synthesis ◽  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

An RNA-binding protein called PABPC1 has an important role in determining protein synthesis rates and hypertrophy in the heart.

scholarly journals Translational Regulation of CUG‐BP1 by Polyamines through the RNA‐binding Protein HuR

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Yuhong Cui ◽  
Lan Xiao ◽  
Jaladanki N. Rao ◽  
Tongtong Zou ◽  
Lan Liu ◽  
...  
Keyword(s):  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA-binding protein Orb2 is associated with microcephaly and supports centrosome asymmetry in neural stem cells

2021 ◽  
Author(s):  
Beverly V. Robinson ◽  
Junnan Fang ◽  
Dipen S. Mehta ◽  
Joseph Buehler ◽  
Dorothy Lerit
Keyword(s):  
Stem Cells ◽  
Neural Stem Cells ◽  
Translational Regulation ◽  
Rna Binding ◽  
Asymmetric Cell Division ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Protein Composition ◽  
Rna Targets ◽  
Stem Cell Pool

To maintain a balance of self-renewal versus neurogenesis, neural stem cells (NSCs) undergo repeated cycles of asymmetric cell division along an invariant polarity axis instructed by centrosomes. During interphase, the NSC centrosomes are defined by marked asymmetries in protein composition and functional activity as microtubule-organizing centers. Here, we show a conserved RNA-binding protein, Orb2, supports centrosome asymmetry in interphase NSCs. While Orb2 localizes to the active apical centrosome, it promotes the transient inactivation of the basal centrosome required for centrosome segregation and spindle morphogenesis. Orb2 is required cell autonomously within NSCs to support centrosome asymmetry and maintenance of the stem cell pool. Conversely, loss of orb2 manifests in microcephaly independent of Orb2 function in NSCs. We suggest Orb2 plays opposing roles in centrosome activation and inactivation, possibly through the translational regulation of multiple mRNA substrates. Bioinformatics uncovers a significant overlap among RNA targets between Drosophila Orb2 and human CPEB4, consistent with a conserved role for CPEB proteins in in centrosome regulation and neurodevelopment.

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