Ask about this productRelated genes to: MSI1 antibody
- Gene:
- MSI1 NIH gene
- Name:
- musashi RNA binding protein 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-07
- Date modifiied:
- 2016-11-09
Related products to: MSI1 antibody
Related articles to: MSI1 antibody
- In vertebrates, two genes, Musashi1 (Msi1) and Musashi2 (Msi2), encode for highly similar Musashi protein paralogs. The Musashi proteins are known to bind to 3'-UTRs and control translation. In photoreceptor cells, the Musashi proteins promote the inclusion of photoreceptor-specific alternative exons by binding to the proximal downstream of their introns. While the Musashi proteins are expressed in various cell types, their role in regulating splicing appears to be confined to photoreceptor cells, where the two proteins have exceptionally high expression levels. To test if the photoreceptor-specific role of MSI1 and MSI2 in splicing is due to their expression levels in photoreceptor cells, we generated combined Msi1 and Msi2 knockouts that progressively reduced the number of Musashi alleles in photoreceptor cells. We analyzed the splicing of photoreceptor-specific exons in the Cc2d2a, Cep290, Prom1, and Ttc8 genes and the function of photoreceptor cells in the knockouts. We found that a single allele from either Msi1 or Msi2 is sufficient to maintain photoreceptor function and support high inclusion levels of the photoreceptor-specific exons. - Source: PubMed
Publication date: 2026/05/14
Jeong BohyeStoilov Peter - Maintenance of pluripotency in embryonic stem cells (ESCs) requires coordinated integration of transcriptional, metabolic, and epigenetic programs. Here, we identify a post-transcriptional regulatory axis linking the RNA-binding protein Musashi-1 (MSI1) to iron dependent DNA demethylation via the ferritin like gene Fthl17c. Genetic ablation of MSI1 and its short isoform MSI1-C in mESCs induced spontaneous differentiation and was accompanied by downregulation of Fthl17 family genes. Among these, Fthl17c was directly bound and stabilized by MSI1, and its depletion reduced intracellular ferrous iron (Fe⁺), impaired ten eleven translocation (TET) enzyme activity, and increased global 5-methylcytosine (5mC) levels. Restoration of Fthl17c expression rescued TET activity, reduced DNA methylation, and reinstated pluripotency associated gene expression, whereas extracellular Fe⁺ supplementation alone was insufficient. In contrast, vitamin C, which preserves redox active Fe⁺, effectively restored DNA demethylation, highlighting the requirement for bioavailable iron in TET mediated epigenetic regulation. Biochemical and imaging analyses further revealed that FTHL17C interacts with TET1 in the nucleus, supporting a role in facilitating iron dependent catalysis. Together, these findings define an MSI1-FTHL17C-Fe⁺-TET axis that integrates post transcriptional control of iron homeostasis with epigenetic remodeling to preserve the pluripotent and plastic state of embryonic stem cells. - Source: PubMed
Publication date: 2026/05/06
Li QianyanLi YiHan JiazhenCheng LimingLin GufaChen Youwei - Neuroblastoma remains a major cause of pediatric cancer mortality and although intensive multimodal treatment strategies have improved survival, they have also led to an increased risk of long-term treatment-related toxicities among survivors. This study aimed to evaluate the potential involvement of (Musashi) Msi1 in neuroblastoma oncogenesis and etoposide treatment response. - Source: PubMed
Cochran Elizabeth DQiao JingboMachchhar ArtiJacobson Jillian CMcCreery SullivanChung Dai H - Musashi RNA-binding proteins are important post-transcriptional regulators of stem cell homeostasis and are known to be involved in viral infections. However, their role in SARS-CoV-2 infection remains largely unknown. Using computational studies, in vivo RNA immunoprecipitation, and biochemical assays, here, we establish that Musashi 1 (Msi1) interacts with viral genomic RNA through direct binding to the SARS-CoV-2 3'UTR. Importantly, binding of Msi1 to the viral 3'UTR results in translational repression that could be mediated by inhibition of poly(A) binding protein. Conversely, Msi1 knockout promotes robust viral replication and increased viral protein expression. Using 2D cell cultures, stem cells, and 3D organoids, we show that depletion of Msi1 in intestinal cells augments infection. This finding explains why the human intestine serves as a reservoir for SARS-CoV-2, in which differentiated enterocytes with negligible Msi1 levels are particularly affected. Contrarily, stem cells, which are enriched for Msi1 expression, are known to be less permissive to SARS-CoV-2 infection despite expressing the entry receptors. Our findings show how translational repression of SARS-CoV-2 by stem cell RNA-binding proteins, such as Msi1, could help evade infection. - Source: PubMed
Ganguli SouravGupta DivyaKadumuri Rajashekar VarmaTandel DixitRamaswamy RajashreeKrishnan Aswathy GDavid Deena TBunk SoumyaChavali SreenivasHarshan Krishnan HarinivasChavali Pavithra L - - Source: PubMed
Jing Hongwei