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Human MBNL1 Protein expressed in HEK-293 Cells - ABIN2725584
Echeverria, Cooper: Muscleblind-like 1 activates insulin receptor exon 11 inclusion by enhancing U2AF65 binding and splicing of the upstream intron. dans Nucleic acids research 2014
Mbnl1(+/-); Mbnl2(+/-) knockout mice with myotonic dystrophy presented with clinical myofibril ultrastructural abnormality and cardiac arrhythmias.
our study uncovered a novel, autoregulatory function of MBNL proteins based on their binding to e1 of MBNL1 transcript. This function might facilitate cellular protection from MBNL protein level fluctuations, which might otherwise lead to adverse effects caused by extreme MBNL content.
Data show that Muscleblind-like 1 (Mbnl1) and Muscleblind-Like 3 (Mbnl3) bind skeletal muscle chloride channel CIC-1 (Clc-1) mRNA.
Depletion of Mbnl1 and/or Mbnl2 reduced localization of hundreds of transcripts, implicating Mbnls in localization of mRNAs to neurites
Sense DMPK RNA foci clearly co-localize with MBNL1 and MBNL2 proteins and accumulate in myotonic dystrophy 1 tissues during development.
MBNL1 overexpression promotes transformation of fibroblasts into myofibroblasts.
These data indicate that MBNL1 plays a conserved role in negatively regulating TGFbeta signaling, and is required for normal valve morphogenesis and homeostasis in vivo.
this study supports a key role for Mbnl1 loss in the initiation of DM1 cardiac disease.
Differential expression of Mbnl1 in development plays a role in alternative splicing of vesicular trafficking genes in postnatal heart development.
Results show that nuclear localization is a major determinant of MBNL1 function. It promotes the nuclear retention of repeat-containing transcripts, which results in repression of aberrant protein expression from the expanded repeats.
depletion of Mbnl proteins in mouse embryo fibroblasts leads to misregulation of thousands of alternative polyadenylation events.
consistent with a central and negative regulatory role for MBNL proteins in pluripotency, their knockdown significantly enhances the expression of key pluripotency genes and the formation of induced pluripotent stem cells during somatic cell reprogramming
MBNL1 overexpression may be a valuable strategy for treating the skeletal muscle features of Myotonic dystrophy .
This analysis identified several hundred splicing events whose regulation depended on Mbnl function in a pattern indicating functional interchangeability between Mbnl1 and Mbnl2.
The sequestration of MBNL1 by CUG(exp) RNA results in aberrant splicing events in the Myotonic dystrophy type 1 brain.
Muscleblind1, but not Dmpk or Six5, contributes to a complex phenotype of muscular and motivational deficits in mouse models of myotonic dystrophy
Conserved developmental stage- and tissue-specific alternative splicing of MBNL transcripts is an important mechanism by which MBNL activity is regulated during embryonic development.
The authors propose that expanded CTG DNA repeats cause two separate effects: loss of Mbnl1 function (disrupting splicing) and loss of another function that disrupts extracellular matrix mRNA regulation, possibly mediated by Mbnl2.
results show that disruption of the mouse Mbnl1 gene leads to muscle, eye, and RNA splicing abnormalities that are characteristic of myotonic dystrophy disease
Results support the hypothesis that the loss of muscleblind-like 1 activity is a primary pathogenic event in the development of RNA missplicing and myotonia in myotonic dystrophy.
RBFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences.
Functional depletion of the alternative splicing factors Muscleblind-like (MBNL 1 and 2) is at the basis of the neuromuscular disease myotonic dystrophy type 1 (DM1). Here, we screen for miRNAs that regulate MBNL1 and MBNL2 in HeLa cells. We thus identify miR-23b and miR-218, and confirm that they downregulate MBNL proteins in this cell line.
For exogenous activation of MBNL transcription, MBNL1 transcription start site T2 seems to be the most suitable target, as the ensuing pre-mRNA is susceptible to both major loops, e1 and e5, and hence, theoretically, following induction each cell in the body could reach the optimal MBNL content.
RAN Translation Regulated by Muscleblind Proteins in Myotonic Dystrophy Type 2
Our work suggests that DM1 patients are at risk for Fuchs' endothelial corneal dystrophy (FECD). DMPK mutations contribute to the genetic burden of FECD but are uncommon. We establish a connection between two repeat expansion disorders converging upon RNA-MBNL1 foci and FECD.
Binding of the MBNL zinc fingers to cardiac troponin T pre-mRNA is specific and relatively simple, unlike the complex multiple dimer-trimer stoichiometries postulated in some previous studies.
Heterozygous missense mutations and one in-frame deletion in MBNL1 were identified in 3 myotonic dystrophy patients.
Nuclear retention of full-length HTT RNA is mediated by splicing factors MBNL1 and U2AF65
muscleblind-like 1 (MBNL1) is a robust suppressor of multiorgan breast cancer metastasis. It binds the 3' untranslated regions of DBNL and TACC1 -two genes that are implicated as metastasis suppressors.
abnormal splicing of DMD exon 78 found in dystrophic muscles of DM1 patients is due to the functional loss of MBNL1 and leads to the re-expression of an embryonic dystrophin in place of the adult isoform.
Reduced RBFOX1 activity in myotonic dystrophy type 1 tissues may amplify several of the splicing alterations caused by the deficiency in MBNL1.
MBNL1 binds with C allelic pre-miR-1307 leading to low expression of miR-1307-3p in colorectal cancer.
The result is consistent with the hypothesis that MBNL proteins are trapped by expanded CUG repeats and inactivated in myotonic dystrophy type 1 (DM1) and that CELF1 is activated in DM1.
Results highlight the importance of RNA binding by MBNL Zinc Finger domains 1 and 2 for splicing regulatory activity, even when the protein is artificially recruited to its regulatory location on target RNAs.
both MBNL1 and MBNL2 are involved in the regulation of Tau exon 2 splicing and the mis-splicing of Tau in DM1 is due to the combined inactivation of both.
MBNL1 and RBFOX2 cooperate to establish a splicing programme involved in pluripotent stem cell differentiation.
MBNL1 is highly mobile and changes localization in response to altered transcription and splicing activity, providing an insight into the sensitivity of the lens to changes in MBNL1 distribution.
MBNL142-43 bind the Src-homology 3 domain of Src family kinases (SFKs) via their proline-rich motifs.
Involved in pre-mRNA alternative splicing regulation. Binds to CUG triplet repeat in RNA (By similarity).
, muscleblind-like (Drosophila)
, muscleblind-like protein 1
, muscleblind-like 1
, triplet-expansion RNA-binding protein