Identification of flotillin-1 as an interacting protein for antisecretory factor.
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.
Johansson
Ewa
E
Institute of Biomedicine, Department of Infectious Diseases, Section of Clinical Bacteriology, Göteborg University, Göteborg, Sweden.
Jonson
Ingela
I
Bosaeus
Mattias
M
Jennische
Eva
E
D002478:Cells, Cultured; D003198:Computer Simulation; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D008958:Models, Molecular; D009479:Neuropeptides / Q000378:metabolism*; D011485:Protein Binding; D020798:Two-Hybrid System Techniques; D015003:Yeasts / Q000235:genetics
D008565:Membrane Proteins; D009479:Neuropeptides; C049628:antisecretory factor; C106354:flotillins