Ask about this productRelated genes to: MBNL1 Blocking Peptide
- Gene:
- MBNL1 NIH gene
- Name:
- muscleblind like splicing regulator 1
- Previous symbol:
- MBNL
- Synonyms:
- KIAA0428, EXP42, EXP40, EXP35, EXP
- Chromosome:
- 3q25.1-q25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-26
- Date modifiied:
- 2018-02-13
Related products to: MBNL1 Blocking Peptide
Related articles to: MBNL1 Blocking Peptide
- - Source: PubMed
Publication date: 2026/04/29
Chen Yi-SuLiu Chao-WeiLin Ying-ChinTsai Chia-YingYang Ching-HuiLin Jung-Chun - The Drosophila activity-regulated cytoskeletal-associated protein (dArc1) can facilitate viral-like synaptic transfer of its own mRNA through dArc1 capsid formation. This transfer promotes synaptic maturation at the Drosophila neuromuscular junction and shows conservation to the mammalian neural synapse through the dArc1 mammalian ortholog, Arc. Recently, we established that dArc1 can interact with several transcripts other than its own in Drosophila including the transcript of muscleblind (Mbl), an RNA splicing factor known to be involved in neuronal and muscle development. Here, we demonstrate this interaction is further conserved to Arc and the mammalian Mbl ortholog Muscleblind Like Splicing Regulator 1 (Mbnl1). In the mouse neuro2a (N2A) cell line, immunoprecipitation of Arc protein enriches for both the Arc and Mbnl1 transcript. Upon differentiation of N2A cells, the ability of Arc to bind its own transcript and Mbnl1 are both abolished while potassium stimulation of these cells restored Arc interactions with both transcripts, indicating that this interaction is enhanced by neuronal activity. This interaction is further conserved to the mammalian central nervous system, where Mbnl1 shows increased colocalization with Arc protein in the dentate gyrus of foot-shocked mice. Furthermore, we demonstrate that both Arc and Mbnl1 RNA can be detected in extracellular vesicles (EVs), and that Mbnl1, unlike the Arc transcript, is not directly encapsulated by Arc protein. We additionally observe MblA crosses the Drosophila NMJ, likely within EVs, and postsynaptic MblA accumulation is dependent on presynaptic pools of dArc1. Taken together, our data suggest that Arc protein interacts with Mbnl1 RNA in an activity-dependent manner and this interaction may facilitate transsynaptic transfer of Mbnl1 RNA through EVs with implications for neurodevelopment. - Source: PubMed
Publication date: 2026/03/10
Zinter MaxXiao CongM'Angale Peter GithureZhao-Shea RubingFreels TimothyTapper AndrewThomson Travis - Muscleblind-like (MBNL) RNA-binding proteins (RBPs) possess modular domains that mediate regulation of alternative splicing and RNA localization. Myotonic Dystrophy Type 1 is a CTG repeat expansion disorder where MBNL is sequestered into intranuclear RNA foci, impairing its function. Previous studies found that MBNL self-associates through its exon 7, but the nature of this interaction is not well understood. We identified a cysteine in MBNL1 exon 7 that enables dimerization through formation of an intermolecular disulfide bond. We likewise demonstrate that MBNL2 dimerizes by forming disulfide bonds between multiple cysteines in its carboxy-terminus. Nucleocytoplasmic fractionation revealed a greater proportion of MBNL1 dimer in the nucleus, suggesting a nuclear function for the MBNL1 dimer. We investigated a connection between MBNL1 dimerization and MBNL1-mediated regulation of alternative splicing. To accomplish this, we mutated the MBNL1 cysteine in question to alanine (C325A) and performed RNAseq. We uncovered novel splicing events sensitive to MBNL1 dimerization. We also found that MBNL1 C325A, when co-expressed with expanded CTG repeats, produces smaller, more numerous foci, suggesting a role for the MBNL1 dimer in maintaining foci integrity. These results provide insight into biological and pathological mechanisms of MBNL1 dimerization and suggest other RBPs might similarly dimerize to regulate function. - Source: PubMed
Publication date: 2026/03/26
Knudson Luke AKosti AdamMoss Kathryn RShi LiangNguyen GiaLinh NJanusz-Kaminska AleksandraZhou Eric XHildebrandt Ryan PWang Eric TBassell Gary J - - Source: PubMed
- Kaposi's sarcoma-associated herpesvirus (KSHV) encodes multiple short and long noncoding RNAs which contribute to viral latency, persistence, host gene regulation, and immune evasion. The Antisense-to-Latency Transcript (ALT) is a ~ 10 kb long noncoding RNA (lncRNA) located on the opposite strand of the major latency-associated region encoding the latency associated nuclear antigen, vCyclin, vFLIP, the Kaposin's and 12 microRNA genes. ALT is a nuclear lncRNA that is lowly expressed during latency, but strongly upregulated during lytic replication. Using RNA antisense purification and quantitative mass spectrometry (RAP-MS) in lytically induced primary effusion lymphoma cells, we identified 51 human and 3 viral proteins that directly interact with ALT. Of these enriched proteins, 48 are splicing factors, including core and alternative splicing proteins, such as U2AF2, PTBP1/2, SRSF1/3 and MBNL1. Interaction and co-localization of ALT was confirmed with various splicing factors in ribonucleoprotein complexes. We further identified that induction of lytic replication in lymphoid and epithelial cells leads to thousands of host gene splicing changes, which are partially restored upon perturbation of ALT expression. Finally, transient knockdown of ALT strongly inhibits viral reactivation and virion production. Hence, by splicing factors interactions, ALT interferes with host gene expression. Our results uncover a novel mechanism that shifts gene expression from the host to the virus late during the viral replication cycle to efficiently produce progeny virus and potentially antagonize host immune defenses. - Source: PubMed
Publication date: 2026/03/26
Hong YuanShekhar RituMcMahon SarahKeil NetanyaBaddoo MelodyWatkins J MontyKeshishian HasmikStanclift CarolineCarr Steven AMunschauer MathiasBurke James MFlemington Erik KRenne Rolf