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J. Harry Caufield

Creating new methods is great for three reasons:
  1. It allows old phenomena to be explored in new ways.
  2. It provides other researchers with more options.
  3. It permits creation of ludicrous acronyms.
A recent paper by Moreno et al. in Molecular Systems Biology is an example of cases 1 and 3. Perhaps it will someday be useful to researchers studying protein-protein interactions, but for now, SPLIFF looks like a good way to visualize interactions found by other assays (i.e., yeast two-hybrid).

But I'm getting ahead of myself. This is a method called SPLIFF. It's about lighting up cells. Somebody got a little carried away with that acronym.

SPLIFF is a Split-Ubiquitin method and indicates protein-protein interactions within cells though the ratio fluorescence produced by two auto-fluorescent reporter proteins. Assays for protein-protein interactions usually use a growth phenotype or a colorimetric reporter to indicate interactions, so SPLIFF may offer more clearly quantifiable, temporally-sensitive results. The authors also show how SPLIFF, like other fluorescence-based methods, can localize interactions within cells. The protein interactions are reportedly detected instantaneously.  Hopefully this method can weed out some of the false-positives in two-hybrid interaction screens.

Moreno, D., Neller, J., Kestler, H., Kraus, J., Dünkler, A., & Johnsson, N. (2013). A fluorescent reporter for mapping cellular protein-protein interactions in time and space Molecular Systems Biology, 9 DOI: 10.1038/msb.2013.3