RNA-protein interactions define most of the processing events that determine the life-cycle of all RNA molecules inside a eukaryotic cell. It has been long known, in fact, that as soon as a RNA molecule emerges from its transcriptional start site it is immediately coated by a huge number of RNA binding proteins (RBPs). These proteins contain a rather wide variety of RNA binding motifs that allow them to compete with each other for more or less specific binding sites upon the RNA sequence. Depending on their localization and interactions strength, the RBPs combinatorially interact with each other and will collectively determine the fate of every RNA in different organs and developmental conditions.
At present, several hundred of these RBPs have been described and studied to a variable extent. The family of Cas13 enzymes are one of the newest members of ever growing list of RBPs. However, recent proteomic analyses have also highlighted the presence of many RNA binding factors that have yet to be characterized. It is now therefore clear that any cell uses a very complex network of RNA protein-interactions in order to regulate and amplify the information that is contained in its genes. In many cases, this complexity in RNA-protein interactions can explain the high level of sophistication that can be observed in higher organisms, especially with regards to brain functions. In-vitro studies using structural and biochemical approaches help to understand the molecular mechanism of a RNA-Protein complex. However, it is a real challenge to study these complexes under in-vitro conditions due to their complex nature.
Unfortunately, this complexity also comes with a price and misregulation in the expression of RNA binding proteins has been increasingly described to be associated with monogenic but also complex human pathologies, such as cancer and Alzheimer disease. Many disease specific mutations in RBPs have been characterized but many more such mutations are yet to be identified for therapeutic development.
For these reasons, we would like to ask our readers to contribute by writing Reviews or submitting Original Research papers on the following topics:
• New modes of RNA-protein interactions.
• Experimental strategies to characterize RNA-protein complexes.
• Development of computational tools to predict RBP binding sites.
• Role played by RBPs in regulating all aspects of pre-mRNA processing, including but not limited to: alternative splicing, editing, stability, transport, polyadenylation, translation, and degradation.
• Emerging connections between human diseases and RBP misregulation.
• New potential therapeutic strategies based on the recovery/inhibition of specific RNA-protein interactions.
• CRISPR-Cas13 mediated RNA targeting (it is relatively hot topic and provides an alternative to RNA interference mechanism).
RNA-protein interactions define most of the processing events that determine the life-cycle of all RNA molecules inside a eukaryotic cell. It has been long known, in fact, that as soon as a RNA molecule emerges from its transcriptional start site it is immediately coated by a huge number of RNA binding proteins (RBPs). These proteins contain a rather wide variety of RNA binding motifs that allow them to compete with each other for more or less specific binding sites upon the RNA sequence. Depending on their localization and interactions strength, the RBPs combinatorially interact with each other and will collectively determine the fate of every RNA in different organs and developmental conditions.
At present, several hundred of these RBPs have been described and studied to a variable extent. The family of Cas13 enzymes are one of the newest members of ever growing list of RBPs. However, recent proteomic analyses have also highlighted the presence of many RNA binding factors that have yet to be characterized. It is now therefore clear that any cell uses a very complex network of RNA protein-interactions in order to regulate and amplify the information that is contained in its genes. In many cases, this complexity in RNA-protein interactions can explain the high level of sophistication that can be observed in higher organisms, especially with regards to brain functions. In-vitro studies using structural and biochemical approaches help to understand the molecular mechanism of a RNA-Protein complex. However, it is a real challenge to study these complexes under in-vitro conditions due to their complex nature.
Unfortunately, this complexity also comes with a price and misregulation in the expression of RNA binding proteins has been increasingly described to be associated with monogenic but also complex human pathologies, such as cancer and Alzheimer disease. Many disease specific mutations in RBPs have been characterized but many more such mutations are yet to be identified for therapeutic development.
For these reasons, we would like to ask our readers to contribute by writing Reviews or submitting Original Research papers on the following topics:
• New modes of RNA-protein interactions.
• Experimental strategies to characterize RNA-protein complexes.
• Development of computational tools to predict RBP binding sites.
• Role played by RBPs in regulating all aspects of pre-mRNA processing, including but not limited to: alternative splicing, editing, stability, transport, polyadenylation, translation, and degradation.
• Emerging connections between human diseases and RBP misregulation.
• New potential therapeutic strategies based on the recovery/inhibition of specific RNA-protein interactions.
• CRISPR-Cas13 mediated RNA targeting (it is relatively hot topic and provides an alternative to RNA interference mechanism).
