Special Issue "RNA-Binding Proteins—Structure, Function, Networks and Disease"
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (31 March 2015)
Prof. Dr. André P. Gerber
Faculty of Health and Medical Sciences, Department of Microbial and Cellular Sciences, School of Biosciences and Medicine, University of Surrey, Stag Hill Campus 19 AX 01, Guildford, GU2 7XH, UK
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Interests: posttranscriptional gene regulation; RNA-binding proteins; non-coding RNA; translational control; ribonomics
RNA-binding proteins (RBPs) are key players for the post-transcriptional control of gene expression. They each bind to subpopulations of RNAs and thereby direct and coordinate the fate of all types of RNAs existing in our cells. RBPs control mRNA expression by guiding the processing, localisation, translation and eventual decay; and they collaborate with non-coding RNAs to achieve specific gene regulatory functions. The interest in RBPs is thus steadily increasing, revealing that they comprise a major class of proteins in all kingdoms of life and that they have widespread implications for cell homeostasis and differentiation, in both development and disease.
This issue intends to present up-to-date reviews about all aspects of RNA-binding proteins, providing an orientation point for investigation of this important class of biomolecules. We thus invite submissions of original research manuscripts (although review manuscripts are welcome as well) that cover but are not restricted to four main areas:
- Structural aspects of ribonucleoprotein complexes, RBPs or domains thereof; bioinformatics prediction of RBPs as well as engineering of RBPs and potential applications.
- Molecular functions of RBPs in post-transcriptional control of gene expression, including RNA processing, RNA export/localisation and decay, as well as translational control in eukaryotes or prokaryotes.
- Global-scale analysis of RBPs and their RNA targets; RNA-protein interaction networks and connectivity to other layers of cellular control.
- The role of RBPs in development and disease; transfer into clinical practice and drug development.
Prof. Dr. André P. Gerber
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access quarterly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 650 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- posttranscriptional gene regulation
- RNA binding domain
- RNA binding protein
- Non-coding RNA
- RNA processing
- RNA localization
- RNA decay
- ribonucleoprotein (RNP)
- translational regulation
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Type of Paper: Review
Title: Roles of prolyl isomerases in RNA-mediated gene expression and implications for development of novel therapeutics
Authors: Roopa Thapar
Affiliation: BioSciences at Rice-Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892, USA; E-Mail: firstname.lastname@example.org
Abstract: The peptidyl-prolyl cis-trans isomerases (PPIases) that include immunophilins (cyclophilins and FKBPs) and parvulins (Pin1, Par14, Par17) participate in cell signaling, transcription, pre-mRNA processing and mRNA decay. The human genome encodes 17 cyclophilins, 18 FKBPs and at least 3 parvulins. Immunophilins are receptors for the immunosuppressive drugs cyclosporin A, FK506, and rapamycin that are used in organ transplantation. Pin1 has also been targeted in the treatment of Alzheimer’s disease, asthma, and a number of cancers. While these PPIases are characterized as molecular chaperones, they also act in a nonchaperone manner to promote protein-protein interactions using surfaces outside their active sites. The immunosuppressive drugs act by a gain-of-function mechanism by promoting protein-protein interactions in vivo. Several immunophilins have been identified as components of the splicesosome and are essential for alternative splicing. Pin1 plays roles in transcription and RNA processing by catalyzing conformational changes in the RNA Pol II C-terminal domain. Pin1 also binds several RNA binding proteins such as AUF1, KSRP, HuR, and SLBP that regulate mRNA decay. The functions of ribonucleoprotein associated PPIases are largely unknown. This review highlights the PPIase genes that play roles in RNA-mediated gene expression, providing insight into their structures, functions and mechanisms of action in vivo.
Type of Paper: Review
Title: Gemin5, a Multitasking RNA-binding Protein Involved in IRES-dependent Translation
Authors: David Piñeiro 1,*, Javier Fernandez-Chamorro 2, Rosario Francisco-Velilla 2 and Encarna Martinez-Salas 2
Affiliation: 1 Medical Research Council Toxicology Unit, Lancaster Rd, Leicester LE1 9HN, UK; 2 Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Cientificas-Universidad Autonoma de Madrid, Cantoblanco 28049 Madrid, Spain; E-Mail: email@example.com (D.P.)
Abstract: Gemin5 is a RNA-binding protein that was first identified as a peripheral component of the survival of motor neurons (SMN) complex. This predominantly cytoplasmic protein recognises the small nuclear RNAs (snRNAs) through its WD-repeat domains, allowing assembly of SMN complex into small nuclear ribonucleoproteins (snRNPs). Additionally, the amino terminal end of the protein has been reported to possess cap-binding capacity and to interact with eukaryotic initiation factor 4E (eIF4E). Gemin5 was also shown to down-regulate translation, to be a substrate of the picornavirus L protease, and to interact with viral internal ribosome entry site (IRES) elements via two non-canonical RNA binding sites located at its carboxy-terminal end. All these features link Gemin5 with translation events. Thus, beyond its role in snRNPs biogenesis, Gemin5 appears to be a multitasking protein. In this review, we will summarise the knowledge of Gemin5 functions. We will focus on the function of the protein on translation control and discuss how the proteolysis of this RNA binding protein modulates its repressor effect during picornavirus infection.