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Title: The SMN protein is a key regulator of nuclear architecture in differentiating neuroblastoma cells
Authors: Clelland, Allyson K.
Kinnear, Nicholas P.
Oram, Lisa
Burza, Julie
Sleeman, Judith Elizabeth
Keywords: Cajal body
snRNP maturation
Spinal muscular atrophy
Survival motor neuron
Cajal bodies
Coiled bodies
Spliceosomal SNRNPS
Fluorescent protein
Splicing SNRNPS
Body formation
QH301 Biology
Issue Date: Nov-2009
Citation: 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 . , 10.1111/j.1600-0854.2009.00972.x
Abstract: 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.
Version: Publisher PDF
Status: Peer reviewed
ISSN: 1398-9219
Type: Journal article
Rights: This is an OnlineOpen article available from
Appears in Collections:University of St Andrews Research
Biology Research
Biomedical Sciences Research Complex (BSRC) Research
Institute of Behavioural and Neural Sciences Research

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