Survival motor neuron protein facilitates assembly of stress granules
Copyright policy )Survival motor neuron protein facilitates assembly of stress granules
The survival motor neuron (SMN) protein forms cytoplasmic granules when overexpressed. We report here that SMN co‐localizes with TIA‐1/R and G3BP, protein assemblers of stress granules (SGs), and that SMN is co‐immunoprecipitated with TIA‐1/R, suggesting that SMN granules are SGs. Formation of SMN granules precedes accumulation of TIA‐1/R, indicating that SMN serves as a facilitator of SG formation. However, the exon 7 skipping product, SMNΔ7, is largely retained in the nucleus and forms nuclear granules, indicating that exon 7 is critical for SG formation. Our findings reveal a novel SMN function and possible SG involvement in the pathogenesis of spinal muscular atrophy.
- University of Massachusetts Medical School United States
Motor Neurons, Binding Sites, Hot Temperature, Molecular Sequence Data, RNA-Binding Proteins, Nerve Tissue Proteins, Spinal muscular atrophy, Fibroblasts, Cytoplasmic Granules, Survival motor neuron, Neuroblastoma, TIA-1/R, Mutagenesis, Cell Line, Tumor, Stress granule, Humans, Amino Acid Sequence, Stress, Mechanical, HeLa Cells, Sequence Deletion
Motor Neurons, Binding Sites, Hot Temperature, Molecular Sequence Data, RNA-Binding Proteins, Nerve Tissue Proteins, Spinal muscular atrophy, Fibroblasts, Cytoplasmic Granules, Survival motor neuron, Neuroblastoma, TIA-1/R, Mutagenesis, Cell Line, Tumor, Stress granule, Humans, Amino Acid Sequence, Stress, Mechanical, HeLa Cells, Sequence Deletion
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