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Journal Article

SMN-mediated assembly of RNPs: a complex story

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78385

Meister,  G.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77925

Eggert,  C.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77961

Fischer,  U.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Meister, G., Eggert, C., & Fischer, U. (2002). SMN-mediated assembly of RNPs: a complex story. Trends in Cell Biology, 12(10), 472-478.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6E3A-0
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.