Identification of flotillin-1 as an interacting protein for antisecretory factor

Regul Pept. 2008 Feb 7;146(1-3):303-9. doi: 10.1016/j.regpep.2007.11.005. Epub 2007 Dec 4.


Antisecretory factor (AF) also named S5a/Rpn10 was originally identified through its capacity to inhibit intestinal hypersecretion and was later shown to be a component in the proteasome complex. AF is also a potent anti-inflammatory agent and can act as a neuromodulator. In this study we used yeast two-hybrid screens, with yeast strain PJ692A transformed with the bait vector pGBKT7 (AF aa 1-105) against yeast strain Y187 pretransformed with human brain or placenta cDNA libraries, to identify AF-binding proteins. Flotillin-1 was identified as a specific interacting factor with AF. Immunohistochemistry showed co-localization of AF and flotillin-1 in nervous tissue. Flotillin-1 is an integral membrane protein and a component of lipid rafts, a membrane specialization involved in transport processes. Intracellular AF may affect secretory processes by regulating the localization of signal proteins to lipid rafts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • Computer Simulation
  • Humans
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Neuropeptides / metabolism*
  • Protein Binding
  • Two-Hybrid System Techniques
  • Yeasts / genetics


  • Membrane Proteins
  • Neuropeptides
  • antisecretory factor
  • flotillins