title: SMN-mediated assembly of RNPs: a complex story.
abstract: Although many RNA-protein complexes or ribonucleoproteins (RNPs) assemble spontaneously in vitro, little is known about how they form in the environment of a living cell. Insight into RNP assembly has come unexpectedly from functional analyses of the survival motor neuron (SMN) protein, a gene product that is affected in the neuromuscular disease spinal muscular atrophy. These studies show that the assembly of spliceosomal U-rich small nuclear RNPs in vivo depends on the activity of two large protein complexes, one of which contains the SMN protein. These complexes might also facilitate the assembly of other cellular RNPs.
authors.affiliation: Max-Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152,., Martinsried, Germany.
authors.forename: Gunter
authors.initials: G
authors.lastname: Meister
authors.forename: Christian
authors.initials: C
authors.lastname: Eggert
authors.forename: Utz
authors.initials: U
authors.lastname: Fischer
mesh_terms: D017362:Cyclic AMP Response Element-Binding Protein; D006801:Humans; D009046:Motor Neurons / Q000378:metabolism*; D009134:Muscular Atrophy, Spinal / Q000235:genetics / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins / Q000378:metabolism*; D055532:SMN Complex Proteins
chemical_list: D017362:Cyclic AMP Response Element-Binding Protein; D009419:Nerve Tissue Proteins; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D055532:SMN Complex Proteins