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MBNL2 is a member of the muscleblind protein family which was initially described in Drosophila melanogaster. De plus, nous expédions MBNL2 Anticorps (32) et beaucoup plus de produits pour cette protéine.
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Mbnl1(+/-); Mbnl2(+/-) knockout mice with myotonic dystrophy presented with clinical myofibril ultrastructural abnormality and cardiac arrhythmias.
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.
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
This analysis identified several hundred splicing events whose regulation depended on Mbnl function in a pattern indicating functional interchangeability between Mbnl1 and Mbnl2.
We propose that major pathological features of the myotonic dystrophy brain result from disruption of the MBNL2-mediated developmental splicing program
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.
MBNL2 contribute to the pathogenesis of myotonic dystrophy.
MBNL2 in splicing regulation of specific transcripts, which, when altered, contributes to the myotonic dystrophy phenotype.
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.
Low MBNL2 expression is associated with hepatocellular carcinoma growth and invasion.
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
MBNL proteins promote opposite splicing patterns for cardiac troponin T and insulin receptor alternative exons
MBNL1 and MBNL2 always co-distributed. Functional differences between MBNL1 and MBNL2 have not yet been found
solution structures of both tandem zinc finger (TZF) motifs, TZF12 (comprising ZF1 and ZF2) and TZF34 (ZF3 and ZF4), in MBNL2
This gene is a member of the muscleblind protein family which was initially described in Drosophila melanogaster. This gene encodes a C3H-type zinc finger protein that modulates alternative splicing of pre-mRNAs. Muscleblind proteins bind specifically to expanded dsCUG RNA but not to normal size CUG repeats and may thereby play a role in the pathophysiology of myotonic dystrophy. Several alternatively spliced transcript variants have been described but the full-length natures of only some have been determined.
muscleblind-like protein 2
, muscleblind-like 2
, muscleblind-like protein 1
, muscleblind-like protein-like 39