scholarly journals The Survival of Motor Neuron Protein Acts as a Molecular Chaperone for mRNP Assembly

Cell Reports ◽  
2017 ◽  
Vol 18 (7) ◽  
pp. 1660-1673 ◽  
Author(s):  
Paul G. Donlin-Asp ◽  
Claudia Fallini ◽  
Jazmin Campos ◽  
Ching-Chieh Chou ◽  
Megan E. Merritt ◽  
...  
Keyword(s):  
Motor Neuron ◽  
Molecular Chaperone ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron

scholarly journals A screen for regulators of survival of motor neuron protein levels

2011 ◽  
Vol 7 (8) ◽  
pp. 544-552 ◽  
Author(s):  
Nina R Makhortova ◽  
Monica Hayhurst ◽  
Antonio Cerqueira ◽  
Amy D Sinor-Anderson ◽  
Wen-Ning Zhao ◽  
...  
Keyword(s):  
Motor Neuron ◽  
Protein Levels ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron

A role for the survival of motor neuron protein in mRNP assembly and transport

2016 ◽  
Vol 39 ◽  
pp. 53-61 ◽  
Author(s):  
Paul G Donlin-Asp ◽  
Gary J Bassell ◽  
Wilfried Rossoll
Keyword(s):  
Motor Neuron ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron

scholarly journals Survival of motor neuron protein downregulates miR-9 expression in patients with spinal muscular atrophy

2014 ◽  
Vol 30 (5) ◽  
pp. 229-234 ◽  
Author(s):  
Li-Ting Wang ◽  
Shyh-Shin Chiou ◽  
Yu-Mei Liao ◽  
Yuh-Jyh Jong ◽  
Shih-Hsien Hsu
Keyword(s):  
Spinal Muscular Atrophy ◽  
Motor Neuron ◽  
Muscular Atrophy ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron

Nusinersen in the treatment of 5q spinal muscular atrophy (Sponsor: Biogen GmbH, München)

2020 ◽  
Vol 12 (02) ◽  
pp. 1-24
Keyword(s):  
Motor Neuron ◽  
Motor Neurons ◽  
Antisense Oligonucleotide ◽  
Muscle Function ◽  
Muscular Atrophy ◽  
Smn1 Gene ◽  
Motor Neuron Protein ◽  
Smn Protein ◽  
Survival Of Motor Neuron ◽  
Progressive Weakness

AbstractDue to a mutation in the SMN1 gene on chromosome 5, in 5q-SMA there is a deficiency in the survival of motor neuron protein (SMA) which is essential for motor neurons. This leads to a degeneration of the 2nd motor neuron and progressive weakness and atrophy of the affected muscles. The targeted splicing modulator nusinersen (Spinraza®), an antisense oligonucleotide that binds to the SMN2-RNA, leads to increased production of functional SMN protein. This stabilizes the disease and improves muscle function.

scholarly journals CIM Journal Club: Gene therapy for spinal muscular atrophy Comment on Mendell et al. N Engl J Med 2017;377:1713-22.

2018 ◽  
pp. E31-E33 ◽  
Author(s):  
Raphael Schneider
Keyword(s):  
Gene Therapy ◽  
Spinal Muscular Atrophy ◽  
Motor Neuron ◽  
Viral Vector ◽  
Muscular Atrophy ◽  
Journal Club ◽  
Dna Encoding ◽  
Motor Neuron Diseases ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron

In their landmark paper, Mendell et al. show that infants with spinal muscular atrophy (SMA) reached important motor milestones and survived longer when treated with AVXS-101 (AveXis), a viral vector containing DNA encoding the survival of motor neuron protein (SMN). Patients not only crawled, stood and walked independently, but learned to speak. These results are very encouraging for patients with SMA and offer hope for pediatric and adult patients with other types of motor neuron diseases.

scholarly journals DMA-tudor interaction modules control the specificity of in vivo condensates

2020 ◽  
Author(s):  
Edward M. Courchaine ◽  
Andrew E.S. Barentine ◽  
Korinna Straube ◽  
Joerg Bewersdorf ◽  
Karla M. Neugebauer
Keyword(s):  
Motor Neuron ◽  
Specific Interaction ◽  
Cajal Bodies ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Tudor Domain ◽  
Motor Neuron Protein ◽  
Survival Of Motor Neuron ◽  
Cellular Compartmentalization

SummaryBiomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the ‘survival of motor neuron protein’ (SMN) is required for the formation of three different membraneless organelles (MLOs), we hypothesized that at least one region of SMN employs a unifying mechanism of condensation. Unexpectedly, we show here that SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo, while its two intrinsically disordered regions (IDRs) were not. The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA), and was shared by at least seven additional tudor domains in six different proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping. These findings show that the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition.

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