Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Molecular and Cellular Proteomics |
| Vol/bind | 6 |
| Udgave nummer | 5 |
| Sider (fra-til) | 798-811 |
| Antal sider | 13 |
| ISSN | 1535-9476 |
| DOI | |
| Status | Udgivet - 2007 |
Bibliografisk note
Keywords: Cell Line; Cytoskeletal Proteins; Fragile X Mental Retardation Protein; Humans; Metabolic Networks and Pathways; Microscopy, Atomic Force; Proteomics; RNA, Messenger; RNA-Binding Proteins; RibonucleoproteinsAdgang til dokumentet
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Molecular composition of IMP1 ribonucleoprotein granules. / Jønson, Lars; Vikesaa, Jonas; Krogh, Anders; Nielsen, Lars K; Hansen, Thomas vO; Borup, Rehannah; Johnsen, Anders H; Christiansen, Jan; Nielsen, Finn C.
I: Molecular and Cellular Proteomics, Bind 6, Nr. 5, 2007, s. 798-811.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - Molecular composition of IMP1 ribonucleoprotein granules.
AU - Jønson, Lars
AU - Vikesaa, Jonas
AU - Krogh, Anders
AU - Nielsen, Lars K
AU - Hansen, Thomas vO
AU - Borup, Rehannah
AU - Johnsen, Anders H
AU - Christiansen, Jan
AU - Nielsen, Finn C
N1 - Keywords: Cell Line; Cytoskeletal Proteins; Fragile X Mental Retardation Protein; Humans; Metabolic Networks and Pathways; Microscopy, Atomic Force; Proteomics; RNA, Messenger; RNA-Binding Proteins; Ribonucleoproteins
PY - 2007
Y1 - 2007
N2 - Localized mRNAs are transported to sites of local protein synthesis in large ribonucleoprotein (RNP) granules, but their molecular composition is incompletely understood. Insulin-like growth factor II mRNA-binding protein (IMP) zip code-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 fragile X mental retardation protein granules, processing bodies, and stress granules. Granules were 100-300 nm in diameter and consisted of IMPs, 40 S ribosomal subunits, shuttling heterologous nuclear RNPs, poly(A)-binding proteins, and mRNAs. Moreover granules contained CBP80 and factors belonging to the exon junction complex and lacked eIF4E, eIF4G, and 60 S ribosomal subunits, indicating that embodied mRNAs are not translated. Granules embodied mRNAs corresponding to about 3% of the human embryonic kidney 293 mRNA transcriptome. Messenger RNAs encoding proteins participating in the secretory pathway and endoplasmic reticulum-associated quality control, as well as ubiquitin-dependent metabolism, were enriched in the granules, reinforcing the concept of RNP granules as post-transcriptional operons.
AB - Localized mRNAs are transported to sites of local protein synthesis in large ribonucleoprotein (RNP) granules, but their molecular composition is incompletely understood. Insulin-like growth factor II mRNA-binding protein (IMP) zip code-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 fragile X mental retardation protein granules, processing bodies, and stress granules. Granules were 100-300 nm in diameter and consisted of IMPs, 40 S ribosomal subunits, shuttling heterologous nuclear RNPs, poly(A)-binding proteins, and mRNAs. Moreover granules contained CBP80 and factors belonging to the exon junction complex and lacked eIF4E, eIF4G, and 60 S ribosomal subunits, indicating that embodied mRNAs are not translated. Granules embodied mRNAs corresponding to about 3% of the human embryonic kidney 293 mRNA transcriptome. Messenger RNAs encoding proteins participating in the secretory pathway and endoplasmic reticulum-associated quality control, as well as ubiquitin-dependent metabolism, were enriched in the granules, reinforcing the concept of RNP granules as post-transcriptional operons.
U2 - 10.1074/mcp.M600346-MCP200
DO - 10.1074/mcp.M600346-MCP200
M3 - Journal article
C2 - 17289661
VL - 6
SP - 798
EP - 811
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
SN - 1535-9476
IS - 5
ER -