scholarly journals Scaffold proteins ITSN1 and ITSN2 interact with nuclear RNA-binding proteins

2019 ◽  
Vol 35 (2) ◽  
pp. 81-90 ◽  
Author(s):  
S. V. Pankivskyi ◽  
N. V. Senchenko ◽  
P. B. Busko ◽  
A. V. Rynditch
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Scaffold Proteins ◽  
Nuclear Rna

scholarly journals Quantitative Proteomics to Identify Nuclear RNA-Binding Proteins of Malat1

2020 ◽  
Vol 21 (3) ◽  
pp. 1166 ◽  
Author(s):  
Marian Scherer ◽  
Michal Levin ◽  
Falk Butter ◽  
Marion Scheibe
Keyword(s):  
Quantitative Proteomics ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Full Length ◽  
Interacting Proteins ◽  
Non Coding Rna ◽  
Nuclear Rna ◽  
Long Non Coding Rna ◽  
Shed Light

The long non-coding RNA Malat1 has been implicated in several human cancers, while the mechanism of action is not completely understood. As RNAs in cells function together with RNA-binding proteins (RBPs), the composition of their RBP complex can shed light on their functionality. We here performed quantitative interactomics of 14 non-overlapping fragments covering the full length of Malat1 to identify possible nuclear interacting proteins. Overall, we identified 35 candidates including 14 already known binders, which are able to interact with Malat1 in the nucleus. Furthermore, the use of fragments along the full-length RNA allowed us to reveal two hotspots for protein binding, one in the 5′-region and one in the 3′-region of Malat1. Our results provide confirmation on previous RNA-protein interaction studies and suggest new candidates for functional investigations.

The human RD protein is closely related to nuclear RNA-binding proteins and has been highly conserved

Gene ◽  
1990 ◽  
Vol 90 (2) ◽  
pp. 299-302 ◽  
Author(s):  
Carol S. Surowy ◽  
George Hoganson ◽  
John Gosink ◽  
Kathleen Strunk ◽  
Richard A. Spritz
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Nuclear Rna

Coupling genetics and post-genomic approaches to decipher the cellular splicing code at a systems-wide level

2010 ◽  
Vol 38 (1) ◽  
pp. 237-241 ◽  
Author(s):  
Yilei Liu ◽  
David J. Elliott
Keyword(s):  
Rna Processing ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Eukaryotic Gene Expression ◽  
Nuclear Rna ◽  
Processing Pathways ◽  
Eukaryotic Gene ◽  
Alternatively Spliced ◽  
Nuclear Rna Processing

Nuclear RNA processing is a critical stage in eukaryotic gene expression, and is controlled in part by the expression and concentration of nuclear RNA-binding proteins. Different nuclear RNA-binding proteins are differentially expressed in different cells, helping the spliceosome to decode pre-mRNAs into alternatively spliced mRNAs. Recent post-genomic technology has exposed the complexity of nuclear RNA processing, and is starting to reveal the mechanisms and rules through which networks of RNA-binding proteins can regulate multiple parallel pathways. Identification of multiple parallel processing pathways regulated by nuclear RNA-binding proteins is leading to a systems-wide understanding of the rules and consequences of alternative nuclear RNA processing.

scholarly journals Gestörter Kerntransport und Phasentrennung von RNA-Bindeproteinen

BIOspektrum ◽  
2021 ◽  
Vol 27 (4) ◽  
pp. 365-367
Author(s):  
Saskia Hutten ◽  
Dorothee Dormann
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Phase Separation ◽  
Frontotemporal Dementia ◽  
Nuclear Import ◽  
Binding Proteins ◽  
Molecular Mechanisms ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Nuclear Rna ◽  
Lateral Sclerosis

AbstractAmyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are fatal neurodegenerative disordes, whose underlying molecular mechanisms are only beginning to emerge. A common molecular hallmark of both diseases is the relocalization of nuclear RNA-binding proteins (RBP) into cytoplasmic aggregates. Defects in nuclear import and aberrant phase separation appear to underlie RBP mislocalization and aggregation and could potentially be targeted in future therapies.

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