Related Experiment Video
Updated: Jun 2, 2025

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
Nuclear RNA-binding proteins meet cytoplasmic viruses
Alfredo Castello1, Wael Kamel2
1MRC-University of Glasgow Centre for Virus Research, Glasgow G61 1QH, United Kingdom alfredo.castello@glasgow.ac.uk.
Abstract:
Cytoplasmic viruses interact intricately with the nuclear pore complex and nuclear import/export machineries, affecting nuclear-cytoplasmic trafficking. This can lead to the selective accumulation of nuclear RNA-binding proteins (RBPs) in the cytoplasm. Pioneering research has shown that relocated RBPs serve as an intrinsic defense mechanism against viruses, which involves RNA export, splicing, and nucleolar factors. For instance, the U2 small nuclear ribonucleoprotein (snRNP) relocates to the cytoplasm in infected cells and uses U2 snRNA to interact with viral genomes, repressing viral replication and gene expression. Here, we describe these emerging host-virus interactions and discuss the remaining questions to elucidate their antiviral mechanisms.
Related Concept Videos
Nuclear Export of mRNA
Retrovirus Life Cycles
Leaky Scanning
Intracellular Movement of Viruses and Bacteria
Regulation of Nuclear Protein Sorting
Types of RNA
RNA Performs Diverse...

