The SMN protein is a key regulator of nuclear architecture in differentiating neuroblastoma cells
MetadataShow full item record
The cell nucleus contains two closely related structures, Cajal bodies (CBs) and gems. CBs are the first site of accumulation of newly assembled splicing snRNPs (small nuclear ribonucleoproteins) following their import into the nucleus, before they form their steady-state localization in nuclear splicing speckles. Gems are the nuclear site of accumulation of survival motor neurons (SMNs), an insufficiency of which leads to the inherited neurodegenerative condition, spinal muscular atrophy (SMA). SMN is required in the cytoplasm for the addition of core, Sm, proteins to new snRNPs and is believed to accompany snRNPs to the CB. In most cell lines, gems are indistinguishable from CBs, although the structures are often separate in vivo. The relationship between CBs and gems is not fully understood, but there is evidence that symmetrical dimethylation of arginine residues in the CB protein coilin brings them together in HeLa cells. During neuronal differentiation of the human neuroblastoma cell line SH-SY5Y, CBs and gems increase their colocalization, mimicking changes seen during foetal development. This does not result from alterations in the methylation of coilin, but from increased levels of SMN. Expression of exogenous SMN results in an increased efficiency of snRNP transport to nuclear speckles. This suggests different mechanisms are present in different cell types and in vivo that may be significant for the tissue-specific pathology of SMA.
Clelland , A K , Kinnear , N P , Oram , L , Burza , J & Sleeman , J E 2009 , ' The SMN protein is a key regulator of nuclear architecture in differentiating neuroblastoma cells ' Traffic , vol 10 , no. 11 , pp. 1585-1598 . DOI: 10.1111/j.1600-0854.2009.00972.x
This is an OnlineOpen article available from http://onlinelibrary.wiley.com
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.