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
- Head and neck squamous cell carcinoma (HNSCC) is frequently managed with radiotherapy, but the emergence of radioresistant cancer cells with cancer stem cell (CSC) properties remains a major clinical obstacle. Here, we established a radioresistant FaDu cell line (F-IRR) by repeated fractionated irradiation to investigate the molecular basis of radiation resistance in HNSCC. Irradiated colony-forming assays confirmed the radioresistant phenotype of F-IRR cells. Although F-IRR cells proliferated more slowly than parental cells, they exhibited markedly enhanced CSC activity, as demonstrated by sphere formation, limiting dilution, and soft agar assays. Among multiple stem cell-associated markers, Musashi-1 (MSI1)-an ribonucleic acid (RNA)-binding protein with established roles in CSC maintenance-was the most prominently upregulated, as confirmed by western blot, reverse transcription-polymerase chain reaction (RT-PCR), and immunocytochemistry. Functional studies demonstrated that siRNA-mediated knockdown of MSI1 suppressed stemness and radioresistance in F-IRR cells, whereas stable MSI1 overexpression in parental FaDu and CAL27 cells conferred enhanced stemness and radiation resistance. RNA sequencing and pathway analysis identified hyperactivation of the mitogen-activated protein kinase (MAPK) pathway in F-IRR cells, and targeted inhibition experiments showed that the c-Jun N-terminal kinase (JNK) signaling pathway was the primary upstream regulator of MSI1 expression. JNK inhibition with SP600125 reduced MSI1 levels and attenuated stemness and radioresistance in F-IRR cells. In vivo xenograft experiments further confirmed that F-IRR cells possessed greater tumorigenic potential and radioresistance than parental cells, with high expression of MSI1 and phospho-JNK in tumor tissues. Collectively, these findings identify the JNK-MSI1 axis as a critical driver of CSC-mediated radioresistance in HNSCC and a promising therapeutic target for overcoming treatment failure. - Source: PubMed
Publication date: 2026/09/02
Kang Na-EunJung Chan-WoongKim Yun-JuChi Sung-GilKim Jeong-YubPark Myung-Jin - The RNA-binding proteins Musashi1 and Musashi2 (MSI1 and MSI2) regulate stem cell function and tissue plasticity by modulating mRNA translation. While typically known as translational repressors, the MSI1 and MSI2 proteins can also act as context-dependent activators of mRNA translation, although the mechanism of MSI-mediated translational activation is unknown. Here, we identify Embryonic Lethal Abnormal Vision-like (ELAVL) proteins as essential co-regulators of MSI1-dependent translational activation. In oocytes, antisense oligonucleotide knockdown of inhibited progesterone-stimulated maturation and blocked polyadenylation and translation of key MSI target mRNAs, including the and mRNAs. Exogenous expression of ELAVL4 rescued these defects, confirming its necessity for maturation and cell cycle progression. Mechanistically, we determined that the ELAVL4 C-terminal domain interacts with the N-terminal RNA recognition motifs of MSI1 in an RNA-independent manner. Mass spectrometry and functional assays revealed this interaction is evolutionarily conserved: mouse ELAVL1 interacts with MSI1 in the pituitary, and human ELAVL1 rescues -depleted oocytes. Furthermore, knockdown of in a mammalian cell line abrogated MSI-dependent translational activation of a pituitary 3' UTR mRNA reporter. Our results establish a conserved mechanism where ELAVL family members interact with MSI to promote MSI-dependent mRNA translational activation. - Source: PubMed
Publication date: 2026/07/31
Bronson KatherineReddick Milla MMacnicol Kenzie BBolen ColeHardy LindaLagasse AlexOdle Angela KChilds Gwen VMacNicol Melanie CMacNicol Angus M - To investigate the transcriptional profiling of ocular surface ectoderm (OSE) derived from human embryonic stem cells (hESC), and identified CACNG6 and AQP3 as the surface markers of OSE. - Source: PubMed
Publication date: 2026/08/18
Sun LuLi Yu-MingSong Yu-WenYang Yi-ChenDuan LianGao YangLi Jian-XinYu Yan-KunPang Kun-PengDang Guang-FuZhang Can-Wei - Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that various of the flow cytometry plots featured in Fig. 6A subsequently appeared in six papers written by different authors at different research institutes that were published in the years 2017‑8, one of which has since been retracted (a paper in ). Furthermore, the possible duplication of a western band for the Msi‑1 experiments shown in Fig. 7B was also noted on p. 643, where the same data were apparently used to present two different experimental conditions. The authors were contacted by the Editorial Office to offer an explanation for the issues described above, and they have replied to say that, since this article is old, the digitized raw data for this paper were discarded in accordance with the institute's data retention policy after the mandated retention period; moreover, the authors maintain full confidence in the validity and reproducibility of their overall findings. Owing to the fact that the Editorial Office has been made aware of potential issues surrounding the scientific integrity of this paper, however, we are issuing an Expression of Concern to notify readers of this potential problem. [International Journal of Molecular Medicine 35: 637‑644, 2015; DOI: 10.3892/ijmm.2015.2075]. - Source: PubMed
Publication date: 2026/07/24
Xue TaoWei LiZha Ding-JunQiao LiLu Lian-JunChen Fu-QuanQiu Jian-Hua - The RNA-binding proteins Musashi1 and Musashi2 (MSI1 and MSI2) regulate stem cell function and tissue plasticity by modulating mRNA translation. While typically known as translational repressors, the MSI1 and MSI2 proteins can also act as context-dependent activators of mRNA translation, although the mechanism of MSI-mediated translational activation are unknown. Here, we identify Embryonic Lethal Abnormal Vision-like (ELAVL) proteins as essential co-regulators of MSI1-dependent translational activation. In oocytes, antisense oligonucleotide knockdown of inhibited progesterone-stimulated maturation and blocked polyadenylation and translation of key MSI target mRNAs, including the and mRNAs. Exogenous expression of ELAVL4 rescued these defects, confirming its necessity for maturation and cell cycle progression. Mechanistically, we determined that the ELAVL4 C-terminal domain interacts with the N-terminal RNA recognition motifs of MSI1 in an RNA-independent manner. Mass spectrometry and functional assays revealed this interaction is evolutionarily conserved: mouse ELAVL1 interacts with MSI1 in the pituitary, and human ELAVL1 rescues -depleted oocytes. Furthermore, knockdown of in a mammalian cell line abrogated MSI-dependent translational activation of a pituitary 3' UTR mRNA reporter. Our results establish a conserved mechanism where ELAVL family members interact with MSI to promote MSI-dependent mRNA translational activation. - Source: PubMed
Publication date: 2026/07/02
Bronson KatherineReddick Milla MMacNicol Kenzie BBolen ColeHardy LindaLagasse AlexOdle Angela KChilds Gwen VMacNicol Melanie CMacNicol Angus M