期刊
MOLECULAR CELL
卷 16, 期 2, 页码 223-234出版社
CELL PRESS
DOI: 10.1016/j.molcel.2004.09.024
关键词
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资金
- NIGMS NIH HHS [GM53034, R01 GM053034-09] Funding Source: Medline
- NINDS NIH HHS [NS41617, R01 NS041617-05] Funding Source: Medline
Cytoplasmic assembly of Sm-class small nuclear ribonucleoproteins (snRNPs) is a central process in eukaryotic gene expression. A large macromolecular complex containing the survival of motor neurons (SMN) protein is required for proper snRNP assembly in vivo. Defects in SMN function lead to a human neuromuscular disorder, spinal muscular atrophy (SMA). SMN protein localizes to both nuclear and cytoplasmic compartments, and a reduction in nuclear levels of SMN is correlated with the disease. The mechanism of SMN nuclear import, however, is unknown. Using digitonin-permeabilized cells, we show that SMN import depends on the presence of Sm snRNPs. Conversely, import of labeled U1 snRNPs was SMN complex dependent. Thus, import of SMN and U snRNPs are coupled in vitro. Furthermore, we identify nuclear import defects in SMA patient-derived SMN mutants, uncovering a potential mechanism for SMN dysfunction.
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