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Volkanoska, S.

Publications and source records attributed to Volkanoska, S..

2 recordsLinked to original sources

A point mutation in the nuclear speckle protein and splicing factor SRRM2 is associated with amyotrophic lateral sclerosis and causes dysregulation of synapse-associated genes

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by the progressive loss of motor neuron function. ALS is a multifactorial disease which can originate from complex genetic and environmental factors. The identification of risk factors and their molecular contribution to ALS expand our understanding of the disease mechanism. Here, we describe a family with dominantly inherited degeneration, which carries a mutation in the serine/arginine repetitive matrix 2 gene (SRRM2). SRRM2 is essential for nuclear speckle formation and a constitutive member of the RNA splicing machinery. To investigate how the mutation in SRRM2 contributed to the ALS pathogenesis, we examined its effect on a model cell line, where the point mutation was introduced in the endogenous gene. Surprisingly, we found that the resulting single amino acid exchange led to the loss of one protein-protein interaction, between SRRM2 and the splicing factor ACIN1. Transcriptome studies further revealed wide-spread differential gene expression, which converged on the dysregulation of synapse-associated pathways. Together, our findings identify SRRM2 as a novel ALS risk factor and provide mechanistic insights into how its mutation can be linked to ALS pathology.

molecular biology↗

RARS1 integration into the multisynthetase complex is crucial for mammalian brain development

Aminoacyl tRNA synthetases occupy a central role in protein synthesis by charging tRNAs with their cognate amino acid. Eight aminoacyl-tRNA synthetases with nine enzymatic activities form a large protein complex but the breadth of functions mediated by the multisynthetase complex remains elusive. Neurological disorders have been associated with mutations within the domain tethering Arginyl-tRNA synthetase (RARS1) to the multisynthetase complex, which offers an interesting bridge between protein synthesis and neurodevelopment. To interrogate this connection, we developed a mouse model where RARS1 is excluded from the multisynthetase complex in the forebrain. We observed profound disruptions in neural development as attested by drastically reduced forebrain size and behavioral deficits. At the molecular level, neurodevelopmental and ribosomal genes were dysregulated. Finally, the subcellular localization of RARS1 and its colocalization with other translational machinery components were perturbed. Altogether, our results reveal the necessity of RARS1 integration in the multisynthetase complex for proper neurodevelopment.

molecular biology↗