p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum

@article{Cui2012p180PT,
  title={p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum},
  author={X. Cui and H. Zhang and Alexander F Palazzo},
  journal={PLoS Biology},
  year={2012},
  volume={10}
}
The localization of many secretory mRNAs to the endoplasmic reticulum does not require ribosomes or translation, but is instead promoted by p180, an abundant, membrane-bound protein that likely binds directly to mRNA. 
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References

SHOWING 1-10 OF 70 REFERENCES
Hierarchical regulation of mRNA partitioning between the cytoplasm and the endoplasmic reticulum of mammalian cells
TLDR
It is revealed that mRNAs are partitioned between the cytosol and endoplasmic reticulum (ER) compartments in a hierarchical manner and a prominent role for the ER in global protein synthesis is identified. Expand
Identification of a ribosome receptor in the rough endoplasmic reticulum
TLDR
Isolation of this domain has led to the identification, purification and characterization of the intact ribosome receptor, as well as its functional reconstitution into lipid vesicles. Expand
Translocation of proteins across the endoplasmic reticulum
  • S. Simon
  • Medicine, Biology
  • Current Opinion in Cell Biology
  • 1993
TLDR
The roles of the signal recognition particle and its receptor have been understood in greater detail; many membrane components responsible for translocation have been identified; and insight has been gained into how proteins cross membranes. Expand
Retention of mRNA on the endoplasmic reticulum membranes after in vivo disassembly of polysomes by an inhibitor of initiation
TLDR
Results add support to the conclusion that, in human fibroblasts, mRNA is bound directly to ER membranes, independently of the ribosomes and nascent polypeptide chains. Expand
ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane
TLDR
The cryo-EM structure of a ribosome–ERj1p complex is presented, revealing how ERj 1p coordinates the ribosomes at the membrane and how allosteric effects may mediate ERj1s regulatory activity. Expand
Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180
TLDR
Evidence is provided that p180 is required to form translationally active polysome/translocon complexes on the ER membrane, and plays a pivotal role in highly efficient biosynthesis on theER membrane through facilitating polysome formation in professional secretory cells. Expand
ERj1p has a basic role in protein biogenesis at the endoplasmic reticulum
TLDR
Another charged oligopeptide within the cytosolic domain of ERj1p mediates binding of the nuclear import factor importin β and import into the nucleus, thereby paving the way for subsequent action on genomic DNA. Expand
Characterization of the rough endoplasmic reticulum ribosome-binding activity
TLDR
It is reported here that ribosome-binding site activity quantitatively solubilized from rough endoplasmic reticulum membranes does not cofractionate with ERpl80, and fractionates as a much smaller, positively charged protein. Expand
Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans
TLDR
The data demonstrate evolutionary conservation of Sec62/Sec63 interaction and indicate that in the course of evolution Sec62 of vertebrates has gained the additional function to interact with ribosomes. Expand
Translation-Independent Localization of mRNA in E. coli
TLDR
It is reported that certain messenger RNAs in Escherichia coli are targeted to the future destination of their encoded proteins, cytoplasm, poles, or inner membrane in a translation-independent manner. Expand
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5
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