Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells
2006
Studying Dimer Formation of Signal Peptide Peptidase in Cells
Sample size: 26
publication
Evidence: high
Author Information
Author(s): Nyborg Andrew C, Herl Lauren, Berezovska Oksana, Thomas Anne V, Ladd Thomas B, Jansen Karen, Hyman Bradley T, Golde Todd E
Primary Institution: Mayo Clinic Jacksonville
Hypothesis
Does signal peptide peptidase (SPP) exist as a monomer or dimer in vivo?
Conclusion
The study provides strong evidence that signal peptide peptidase forms dimers in intact cells.
Supporting Evidence
- Fluorescence lifetime imaging microscopy (FLIM) showed that SPP molecules are in close proximity.
- Tagged SPP constructs were shown to be proteolytically active.
- Significant decreases in donor fluorophore lifetime indicated dimer formation.
- SPP dimerization was confirmed in both live and fixed cells.
Takeaway
The researchers looked at a protein called SPP to see if it sticks together in pairs, and they found that it does!
Methodology
Fluorescence lifetime imaging microscopy (FLIM) was used to assess the proximity of tagged SPP constructs in living cells.
Limitations
The study does not clarify whether SPP functions as a dimer or monomer in terms of activity.
Statistical Information
P-Value
< 0.001
Statistical Significance
p<0.001
Digital Object Identifier (DOI)
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