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MLP1 Mlp1p

Mlp1, MBNL2, Mlp1p
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. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: EXP, CAN, SET, DM2, Nucleoporin
Papers on Mlp1
The nuclear basket mediates perinuclear mRNA scanning in budding yeast.
Zenklusen et al., Montréal, Canada. In J Cell Biol, Jan 2016
Deletion or mutation of the nuclear basket proteins MLP1/2 or the mRNA binding protein Nab2 changes the scanning behavior of mRNPs at the nuclear periphery, shortens residency time at nuclear pores, and results in frequent release of mRNAs back into the nucleoplasm.
Genomic profiling screens small molecules of metastatic prostate carcinoma.
Sun et al., Beijing, China. In Oncol Lett, Sep 2015
In addition, KPNA4, SYT1, PLCB1, SPRED1, MBNL2, RNF165, MEF2C, MBNL1, ZFP36L1 and CELF2, were found to be likely to play significant roles in the process of metastatic prostate carcinoma.
MBNL Sequestration by Toxic RNAs and RNA Misprocessing in the Myotonic Dystrophy Brain.
Swanson et al., Gainesville, United States. In Cell Rep, Sep 2015
MBNL2 binds directly to DM repeat expansions in the brain, resulting in depletion from its normal RNA targets with downstream effects on alternative splicing and polyadenylation.
scaRNAs regulate splicing and vertebrate heart development.
Bittel et al., Miyazaki, Japan. In Biochim Biophys Acta, Aug 2015
We used primary cells derived from the RV of infants with TOF to show a direct link between scaRNA levels and splice isoforms of several genes that regulate heart development (e.g., GATA4, NOTCH2, DAAM1, DICER1, MBNL1 and MBNL2).
Sense and Antisense DMPK RNA Foci Accumulate in DM1 Tissues during Development.
Gourdon et al., Paris, France. In Plos One, 2014
Sense DMPK RNA foci clearly co-localized with MBNL1 and MBNL2 proteins.
SW1PerS: Sliding windows and 1-persistence scoring; discovering periodicity in gene expression time series data.
Harer et al., Durham, United States. In Bmc Bioinformatics, 2014
These genes are BOP3, CDC10, YIL108W, YER034W, MLP1, PAC2 and RTT101.
Loss of MBNL leads to disruption of developmentally regulated alternative polyadenylation in RNA-mediated disease.
Swanson et al., Gainesville, United States. In Mol Cell, 2014
Although MBNL1 and MBNL2 bind to nascent transcripts to regulate alternative splicing during muscle and brain development, another major binding site for the MBNL protein family is the 3' untranslated region of target RNAs.
Tau exon 2 responsive elements deregulated in myotonic dystrophy type I are proximal to exon 2 and synergistically regulated by MBNL1 and MBNL2.
Caillet-Boudin et al., Lille, France. In Biochim Biophys Acta, 2014
We therefore used new Tau minigenes that we developed for this purpose to determine how MBNL1 and MBNL2 interact to regulate Tau exon 2 splicing.
The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome.
Strambio-De-Castillia et al., Bellinzona, Switzerland. In Mol Biol Cell, 2013
We show that the yeast proteins Mlp1p and Mlp2p are necessary components of the nuclear basket and that they also embed the NPC within a dynamic protein network, whose extended interactome includes the spindle organizer, silencing factors, the proteasome, and key components of messenger ribonucleoproteins (mRNPs).
Two enhancers control transcription of Drosophila muscleblind in the embryonic somatic musculature and in the central nervous system.
Artero et al., Valencia, Spain. In Plos One, 2013
In humans, sequestration of Muscleblind-like proteins MBNL1 and MBNL2 has been implicated in degenerative disorders, particularly expansion diseases such as myotonic dystrophy type 1 and 2. Drosophila muscleblind was previously shown to be expressed in embryonic somatic and visceral muscle subtypes, and in the central nervous system, and to depend on Mef2 for transcriptional activation.
MBNL proteins repress ES-cell-specific alternative splicing and reprogramming.
Blencowe et al., Toronto, Canada. In Nature, 2013
Here we identify the muscleblind-like RNA binding proteins, MBNL1 and MBNL2, as conserved and direct negative regulators of a large program of cassette exon alternative splicing events that are differentially regulated between ES cells and other cell types.
Transcriptome-wide regulation of pre-mRNA splicing and mRNA localization by muscleblind proteins.
Burge et al., Cambridge, United States. In Cell, 2012
This analysis identified several hundred splicing events whose regulation depended on Mbnl function in a pattern indicating functional interchangeability between Mbnl1 and Mbnl2.
Muscleblind-like 2-mediated alternative splicing in the developing brain and dysregulation in myotonic dystrophy.
Swanson et al., Gainesville, United States. In Neuron, 2012
We propose that major pathological features of the myotonic dystrophy brain result from disruption of the MBNL2-mediated developmental splicing program
Aberrant alternative splicing and extracellular matrix gene expression in mouse models of myotonic dystrophy.
Ares et al., Santa Cruz, United States. In Nat Struct Mol Biol, 2010
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.
Conserved developmental alternative splicing of muscleblind-like (MBNL) transcripts regulates MBNL localization and activity.
Ladd et al., Cleveland, United States. In Rna Biol, 2010
Conserved developmental stage- and tissue-specific alternative splicing of MBNL transcripts is an important mechanism by which MBNL activity is regulated during embryonic development.
Muscleblind-like 2: circadian expression in the mammalian pineal gland is controlled by an adrenergic-cAMP mechanism.
Klein et al., Bethesda, United States. In J Neurochem, 2009
Pineal Mbnl2 transcripts and protein levels exhibit marked circadian rhythms; both are neurally regulated by an adrenergic/cyclic adenosine monophosphate (cAMP) mechanism.
The Muscleblind family of proteins: an emerging class of regulators of developmentally programmed alternative splicing.
Artero et al., Valencia, Spain. In Differentiation, 2006
Human Muscleblind homologs MBNL1, MBNL2 and MBNL3 promote inclusion or exclusion of specific exons on different pre-mRNAs by antagonizing the activity of CUG-BP and ETR-3-like factors (CELF proteins) bound to distinct intronic sites.
RNA-dependent integrin alpha3 protein localization regulated by the Muscleblind-like protein MLP1.
Hsu et al., Charleston, United States. In Nat Cell Biol, 2005
We show that localized expression of the integrin alpha3 protein is regulated at the level of RNA localization by the human homologue of Drosophila Muscleblind, MLP1/MBLL/MBNL2, a unique Cys3His zinc-finger protein.
Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1.
Nehrbass et al., Paris, France. In Cell, 2004
Here, we show that retention of intron-containing mRNAs in yeast is mediated by perinuclearly located Mlp1.
Nuclear pore complexes in the organization of silent telomeric chromatin.
Nehrbass et al., Paris, France. In Nature, 2000
Here we show that nuclear-pore-complex extensions formed by the conserved TPR homologues Mlp1 and Mlp2 are responsible for the structural and functional organization of perinuclear chromatin.
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