Document Detail


The survival of motor neurons protein determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy.
MedLine Citation:
PMID:  15964810     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Reduction of the survival of motor neurons (SMN) protein levels causes the motor neuron degenerative disease spinal muscular atrophy, the severity of which correlates with the extent of reduction in SMN. SMN, together with Gemins 2 to 7, forms a complex that functions in the assembly of small nuclear ribonucleoprotein particles (snRNPs). Complete depletion of the SMN complex from cell extracts abolishes snRNP assembly, the formation of heptameric Sm cores on snRNAs. However, what effect, if any, reduction of SMN protein levels, as occurs in spinal muscular atrophy patients, has on the capacity of cells to produce snRNPs is not known. To address this, we developed a sensitive and quantitative assay for snRNP assembly, the formation of high-salt- and heparin-resistant stable Sm cores, that is strictly dependent on the SMN complex. We show that the extent of Sm core assembly is directly proportional to the amount of SMN protein in cell extracts. Consistent with this, pulse-labeling experiments demonstrate a significant reduction in the rate of snRNP biogenesis in low-SMN cells. Furthermore, extracts of cells from spinal muscular atrophy patients have a lower capacity for snRNP assembly that corresponds directly to the reduced amount of SMN. Thus, SMN determines the capacity for snRNP biogenesis, and our findings provide evidence for a measurable deficiency in a biochemical activity in cells from patients with spinal muscular atrophy.
Authors:
Lili Wan; Daniel J Battle; Jeongsik Yong; Amelie K Gubitz; Stephen J Kolb; Jin Wang; Gideon Dreyfuss
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  25     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2005 Jul 
Date Detail:
Created Date:  2005-06-20     Completed Date:  2005-08-02     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5543-51     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute, Department of Biochemistry & Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Biotinylation
Cell Extracts / analysis
Cell Line
Cell Line, Transformed
Cell Transformation, Viral
Chickens
Cyclic AMP Response Element-Binding Protein / metabolism*
Cytoplasm / chemistry
Fibroblasts / cytology,  metabolism
Hela Cells
Herpesvirus 4, Human
Humans
Kinetics
Models, Biological
Motor Neurons / metabolism
Muscular Atrophy, Spinal / genetics*,  pathology
Nerve Tissue Proteins / deficiency*,  metabolism*
Phosphorus Radioisotopes / diagnostic use
Protein Binding
RNA, Small Nuclear / metabolism
RNA-Binding Proteins / metabolism*
Ribonucleoproteins, Small Nuclear / analysis,  metabolism*
SMN Complex Proteins
Sensitivity and Specificity
Transcription, Genetic
Chemical
Reg. No./Substance:
0/Cell Extracts; 0/Cyclic AMP Response Element-Binding Protein; 0/Nerve Tissue Proteins; 0/Phosphorus Radioisotopes; 0/RNA, Small Nuclear; 0/RNA-Binding Proteins; 0/Ribonucleoproteins, Small Nuclear; 0/SMN Complex Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of...
Next Document:  Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyel...