N-Terminal Acetylation Inhibits Protein Targeting to the Endoplasmic Reticulum
2011
N-Terminal Acetylation Inhibits Protein Targeting to the Endoplasmic Reticulum
publication
Evidence: high
Author Information
Author(s): Gabriella M. A. Forte, Martin R. Pool, Colin J. Stirling
Primary Institution: University of Manchester
Hypothesis
Does N-terminal acetylation affect the targeting of proteins to the endoplasmic reticulum?
Conclusion
N-terminal acetylation inhibits the translocation of secretory proteins to the endoplasmic reticulum.
Supporting Evidence
- N-terminal acetylation is a major determinant in protein sorting in eukaryotes.
- Mutations in secretory signal sequences that led to their acetylation resulted in mis-sorting to the cytosol.
- Acetylation blocks secretory substrate interaction with the translocon.
Takeaway
This study found that proteins meant to go to the endoplasmic reticulum shouldn't be modified at their start, or they won't get there. It's like putting a sticker on a letter that makes it go to the wrong address.
Methodology
The study used a combination of bioinformatic and experimental approaches to analyze the N-terminal processing of signal sequences in yeast.
Statistical Information
P-Value
p<0.0001
Statistical Significance
p<0.0001
Digital Object Identifier (DOI)
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