Abstract
Gemin5 is a RNA-binding protein (RBP) 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 the 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 the eukaryotic initiation factor 4E (eIF4E). Gemin5 was also shown to downregulate translation, to be a substrate of the picornavirus L protease and to interact with viral internal ribosome entry site (IRES) elements via a bipartite non-canonical RNA-binding site located at its carboxy-terminal end. These features link Gemin5 with translation control events. Thus, beyond its role in snRNPs biogenesis, Gemin5 appears to be a multitasking protein cooperating in various RNA-guided processes. In this review, we will summarise current knowledge of Gemin5 functions. We will discuss the involvement of the protein on translation control and propose a model to explain how the proteolysis fragments of this RBP in picornavirus-infected cells could modulate protein synthesis.
Highlights
Ribonucleic acid-binding proteins (RBPs) are important players of gene expression control in all organisms, from Bacteria and Archaea to Eukarya
Presumably unrelated to its RNA-interacting capacity, Gemin5 has been reported to be a scaffold protein, playing a role in the assembly process of the complex containing apoptosis signal-regulating kinase 1 (ASK1), stress-activated protein kinase 1 (SEK1) and c-Jun NH2-terminal kinase 1 (JNK1) proteins, which are involved in H2O2 and tumour necrosis factor- (TNF) driven apoptosis [31]
The distinct roles of Gemin5 are related to its capacity to recognise different RNA targets, the small nuclear RNAs (snRNAs), the cap residue (m7 GpppN) of mRNAs or a specific domain within the foot-and-mouth disease virus (FMDV) internal ribosome entry site (IRES) element
Summary
Ribonucleic acid-binding proteins (RBPs) are important players of gene expression control in all organisms, from Bacteria and Archaea to Eukarya. A large number of the proteins recently described as RBPs were previously shown to participate in cell metabolism pathways and other cellular events, unrelated to RNA life span. This is an indication of the multifunctionality of RBPs. the diversity of activities performed by RBPs can be indicative of their property to link processes occurring in the nuclear and the cytoplasmic compartment of the cell, as exemplified by RNA splicing factors, RNA transport and translation. The presence of non-canonical RNA-binding sites (RBSs) appears to be a feature of many of the newly discovered RBPs. Proteins performing the same function in organisms belonging to different kingdoms are evolutionary conserved.
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