Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control.
Gemin5
RNA-binding protein
SMA
SMN
reprogramming
translation control
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
29 May 2020
29 May 2020
Historique:
received:
30
04
2020
revised:
22
05
2020
accepted:
27
05
2020
entrez:
4
6
2020
pubmed:
4
6
2020
medline:
17
2
2021
Statut:
epublish
Résumé
RNA-binding proteins (RBPs) play a pivotal role in the lifespan of RNAs. The disfunction of RBPs is frequently the cause of cell disorders which are incompatible with life. Furthermore, the ordered assembly of RBPs and RNAs in ribonucleoprotein (RNP) particles determines the function of biological complexes, as illustrated by the survival of the motor neuron (SMN) complex. Defects in the SMN complex assembly causes spinal muscular atrophy (SMA), an infant invalidating disease. This multi-subunit chaperone controls the assembly of small nuclear ribonucleoproteins (snRNPs), which are the critical components of the splicing machinery. However, the functional and structural characterization of individual members of the SMN complex, such as SMN, Gemin3, and Gemin5, have accumulated evidence for the additional roles of these proteins, unveiling their participation in other RNA-mediated events. In particular, Gemin5 is a multidomain protein that comprises tryptophan-aspartic acid (WD) repeat motifs at the N-terminal region, a dimerization domain at the middle region, and a non-canonical RNA-binding domain at the C-terminal end of the protein. Beyond small nuclear RNA (snRNA) recognition, Gemin5 interacts with a selective group of mRNA targets in the cell environment and plays a key role in reprogramming translation depending on the RNA partner and the cellular conditions. Here, we review recent studies on the SMN complex, with emphasis on the individual components regarding their involvement in cellular processes critical for cell survival.
Identifiants
pubmed: 32485878
pii: ijms21113868
doi: 10.3390/ijms21113868
pmc: PMC7311978
pii:
doi:
Substances chimiques
Ribonucleoproteins, Small Nuclear
0
SMN Complex Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministerio de Economia y Competitividad
ID : BFU2017-84492-R
Organisme : Comunidad de Madrid
ID : B2017/BMD-3770
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