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A more recent version of this article appeared on May 1, 2007.
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M600346-MCP200v1
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Submitted on September 5, 2006
Revised on January 17, 2007
Accepted on February 7, 2007

Molecular composition of IMP1 RNP granules

Lars Jønson, Jonas Vikesaa, Anders Krogh, Lars K. Nielsen, Thomas vO. Hansen, Rehannah Borup, Anders H. Johnsen, Jan Christiansen, and Finn C. Nielsen

Clinical Biochemistry, Rigshospitalet, Copenhagen 2100

Corresponding Author: FCN{at}rh.dk

Localized mRNAs are transported to sites of local protein synthesis in large RNP granules, but their molecular composition is incompletely understood. IMP zipcode-binding proteins participate in mRNA localization, and in motile cells IMP-containing granules are dispersed around the nucleus and in cellular protrusions. We isolated the IMP1-containing RNP granules, and found that they represent a unique RNP entity, distinct from neuronal hStaufen and/or FMRP granules, P-bodies and stress-granules. Granules were 100-300 nm in diameter and consisted of IMPs, 40S ribosomal subunits, shuttling hnRNPs, poly(A)-binding proteins, and mRNAs. Moreover, granules contained CBP80 and factors belonging to the exon-junction complex, and lacked eIF4E, eIF4G and 60S ribosomal subunits, indicating that embodied mRNAs are not translated. Granules embodied mRNAs corresponding to about 3% of the HEK293 mRNA transcriptome. Messenger RNAs encoding proteins participating in the secretory pathway and ER-associated quality control, as well as ubiquitin-dependent metabolism, were enriched in the granules, reinforcing the concept of RNP granules as post-transcriptional operons.


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eLetters:

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FMRP and IMP1: Evidence of Absence or Absence of Evidence, Noise in the Protein Interactome
Robert B. Denman
MCP Online, 2 Apr 2007 [Full text]
Response to Denman Letter
Finn C. Nielsen, et al.
MCP Online, 2 Apr 2007 [Full text]

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