ReviewInternational journal of molecular sciences2020
Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control.
Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- A stand-alone ICln release module revealed by deconstructing the SMN complex with engineered Brr1.Nucleic acids research · 2026Article
- circPDE4B downregulation triggers GEMIN5‑dependent translational stress response and autophagy to reduce MAPT pathology.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- A unique mechanism of snRNP core assembly.Nature communications · 2025Article
- PPM1G and its diagnostic, prognostic and therapeutic potential in HCC (Review).International journal of oncology · 2024Review
- Oligomerization regulates the interaction of Gemin5 with members of the SMN complex and the translation machinery.Cell death discovery · 2024Article
- Gene Expression Reprogramming by Citrate Supplementation Reduces HepG2 Cell Migration and Invasion.International journal of molecular sciences · 2024Article
- Expanding the clinical phenotype and genetic spectrum of GEMIN5 disorders: Early-infantile developmental and epileptic encephalopathies.Brain and behavior · 2024Article
- Nucleolar reorganization after cellular stress is orchestrated by SMN shuttling between nuclear compartments.Nature communications · 2023Article
- DDX20: A Multifunctional Complex Protein.Molecules (Basel, Switzerland) · 2023Review
- Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast.iScience · 2023Article
- A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT.Molecular cell · 2023Article
- SMN regulates GEMIN5 expression and acts as a modifier of GEMIN5-mediated neurodegeneration.Acta neuropathologica · 2023Article
- Advances and Breakthroughs in IRES-Directed Translation and Replication of Picornaviruses.mBio · 2023Review
- Article
- Viral RNA Is a Hub for Critical Host-Virus Interactions.Sub-cellular biochemistry · 2023Article
- Mouse models of SMA show divergent patterns of neuronal vulnerability and resilience.Skeletal muscle · 2022Article
- Phosphorylation of T897 in the dimerization domain of Gemin5 modulates protein interactions and translation regulation.Computational and structural biotechnology journal · 2022Article
- The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues.RNA biology · 2021Article
- What Genetics Has Told Us and How It Can Inform Future Experiments for Spinal Muscular Atrophy, a Perspective.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.