Mutational analysis of βCOP (Sec26p) identifies an appendage domain critical for function
2008
Study of βCOP Function and Its Appendage Domain
publication
Evidence: high
Author Information
Author(s): DeRegis Carol J, Rahl Peter B, Hoffman Gregory R, Cerione Richard A, Collins Ruth N
Primary Institution: Cornell University
Hypothesis
Does βCOP contain an adaptin-family appendage and is this domain critical for COPI-coated vesicle formation?
Conclusion
The study confirms that the βCOP appendage domain is essential for its function in COPI vesicle formation.
Supporting Evidence
- The deletion of the appendage domain of Sec26p results in inviability in yeast.
- Over-expression of a truncated Sec26p missing the platform subdomain is dominant negative.
- Random mutagenesis of the Sec26p appendage domain reveals residues critical for function.
Takeaway
The appendage part of a protein called βCOP is really important for helping cells move things around inside them.
Methodology
The study used structural modeling, genetic, biochemical, and cell biological approaches to analyze the βCOP appendage.
Statistical Information
P-Value
p<0.0001
Statistical Significance
p<0.0001
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website