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Data show that the coding sequence of survival of motor neuron 2 (SMN2) differs from that of survival motor neuron 1 (SMN1) by a single nucleotide (c.840C>T) at codon 280 in exon 7.
SMN (show SNRPN Proteins) protein functions in cytoplasmic Sm-core assembly and in the recruitment of the snRNA cap hypermethylase
miR (show MLXIP Proteins)-431 expression was highly increased, and a number of its putative mRNA targets were significantly downregulated in motor neurons after SMN (show STMN1 Proteins) loss. Further, we found that miR (show MLXIP Proteins)-431 regulates motor neuron neurite length by targeting several molecules previously identified to play a role in motor neuron axon outgrowth, including chondrolectin (show CHODL Proteins)
To determine the dependence of oligodendrocyte (OL)on the Smn (show STMN1 Proteins) protein(SMN1), we utilized the Smn (show STMN1 Proteins)-/-;SMN2 (severe) mouse model. Our data suggest that despite the multi-functionality and ubiquitous expression of the Smn (show STMN1 Proteins) protein, it does not play a key role in myelination of the CNS, at least in the context of spinal muscular atrophy pathogenesis.
our studies show that this G-motif represents a novel and essential determinant for axonal localization of the Anxa2 (show ANXA2 Proteins) mRNA mediated by the SMN (show STMN1 Proteins) complex.
A long non-coding RNA (lncRNA) that arises from the antisense strand of SMN (show STMN1 Proteins), SMN (show STMN1 Proteins)-AS1 (show ARSB Proteins), is enriched in neurons and transcriptionally represses SMN (show STMN1 Proteins) expression by recruiting the epigenetic Polycomb (show CBX2 Proteins) repressive complex-2.
SMN1 expression restoration is curative in a spinal muscular atrophy model mice.
Survival motor neuron 1, and survival motor neuron 2, depletion results in increased alternative splicing events.
these results demonstrate that SMN (show STMN1 Proteins) deficiency impacts spleen development and suggests a potential role for immunological development in Spinal muscular atrophy.
Itch monoubiquitinates SMN (show STMN1 Proteins) and monoubiquitination of SMN (show STMN1 Proteins) plays an important role in regulating its cellular localization.
muscle does not appear to require high levels of SMN (show STMN1 Proteins) above what is produced by two copies of SMN2
Findings demonstrate that high expression of SMN (show STMN1 Proteins) in the motor neuron is both necessary and sufficient for proper function of the motor unit. In addition, SMN (show STMN1 Proteins) high expression in neurons and glia has a major impact on survival.
From the computational analysis, it is also possible that SMN's Lys45 and Asp36 act as two electrostatic clips at the SMN (show STMN1 Proteins)-Gemin2 (show GEMIN2 Proteins) complex structure interface
Loss of SMN1 is associated with Spinal muscular atrophy.
A rare variant in exon 7 of SMN1 in three patients affected with type I or type II SMA. Most of the SMN1 transcripts exhibited complete loss of exon 7 in vivo. The variant disrupts Tra2beta1 binding.
These results establish that SMN overexpression in motor neurons slows disease onset and outcome by ameliorating pathological signs in this model of mutant TDP-43-mediated amyotrophic lateral sclerosis (ALS).
A long non-coding RNA (lncRNA) that arises from the antisense strand of SMN (show STMN1 Proteins), SMN (show STMN1 Proteins)-AS1 (show PTGDR Proteins), is enriched in neurons and transcriptionally represses SMN (show STMN1 Proteins) expression by recruiting the epigenetic Polycomb (show CBX2 Proteins) repressive complex-2.
We show that genes of the classical apoptosis pathway are involved in the smn-1-mediated neuronal death, and that this phenotype can be rescued by the expression of human SMN1, indicating a functional conservation between the two orthologs. Finally, we determined that Plastin3/plst-1 genetically interacts with smn-1 to prevent degeneration, and that treatment with valproic acid is able to rescue the degenerative phenotype
SMN (show STMN1 Proteins) functions as a natural inhibitor for IL-1beta (show IL1B Proteins)-induced NF-kappaB (show NFKB1 Proteins) signaling by targeting TRAF6 (show TRAF6 Proteins) and the IKK (show CHUK Proteins) complex.
U12-dependent intron retention is induced upon siRNA knock-down of SMN1 in HeLa cells.
Deletion in SMN1 gene is associated with spinal muscular atrophy.
first cloning and identification of the swine SMN1 gene and show that there is significant sequence homology between swine and human SMN (show SNRPN Proteins) throughout the coding region
This gene is part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. The telomeric and centromeric copies of this gene are nearly identical and encode the same protein. However, mutations in this gene, the telomeric copy, are associated with spinal muscular atrophy\; mutations in the centromeric copy do not lead to disease. The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy. The critical sequence difference between the two genes is a single nucleotide in exon 7, which is thought to be an exon splice enhancer. Note that the nine exons of both the telomeric and centromeric copies are designated historically as exon 1, 2a, 2b, and 3-8. It is thought that gene conversion events may involve the two genes, leading to varying copy numbers of each gene. The protein encoded by this gene localizes to both the cytoplasm and the nucleus. Within the nucleus, the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs). This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN4, and also interacts with several proteins known to be involved in the biogenesis of snRNPs, such as hnRNP U protein and the small nucleolar RNA binding protein. Two transcript variants encoding distinct isoforms have been described.
survival of motor neuron 2, centromeric
, survival motor neuron protein
, ATP-dependent helicase IGHMBP2
, DNA-binding protein SMUBP-2
, antifreeze enhancer-binding protein
, cardiac transcription factor 1
, immunoglobulin S mu binding protein 2
, immunoglobulin mu-binding protein 2
, neuromuscular degeneration
, p110 subunit
, survival of motor neuron protein
, component of gems 1
, survival motor neuron 1 protein
, tudor domain containing 16A
, survival motor neuron 1