Time-resolved quantitative proteomics implicates the core snRNP protein SmB together with SMN in neural trafficking.
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The biogenesis of splicing snRNPs (small nuclear ribonucleoproteins) is a complex process, beginning and ending in the nucleus of the cell but including key stages that take place in the cytoplasm. In particular, the SMN (survival motor neuron) protein complex is required for addition of the core Sm proteins to the snRNP. Insufficiency of SMN results in the inherited neurodegenerative condition, spinal muscular atrophy (SMA). Details of the physical organization of the cytoplasmic stages of snRNP biogenesis are unknown. Here, we use time-resolved quantitative proteomics to identify proteins that associate preferentially with either newly assembled or mature splicing snRNPs. We identified highly mobile SmB protein-trafficking vesicles in neural cells, which are dependent on the cellular levels of SMN and SmB for their morphology and mobility. We propose that these represent a family of related vesicles, some of which play a role in snRNP biogenesis and some that might play more diverse roles in cellular RNA metabolism.
Prescott , A R , Bales , A , James , J , Trinkle-Mulcahy , L & Sleeman , J E 2014 , ' Time-resolved quantitative proteomics implicates the core snRNP protein SmB together with SMN in neural trafficking. ' Journal of Cell Science , vol 127 , no. 4 , pp. 812-827 . DOI: 10.1242/jcs.137703
Journal of Cell Science
© 2014. Published by The Company of Biologists Ltd. This article may be accessed for non-commercial purposes and may not be included in third party article collections without the prior written consent of the Company. The following article appeared in Journal of the Journal of Cell Science and may be found at http://jcs.biologists.org/content/127/4/812
This work is supported in part by the Royal Society via a University Research Fellowship
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