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

Journal article
Authors Ewa Johansson
Ingela Jonson
Mattias Bosaeus
Eva Jennische
Published in Regulatory Peptides
Volume 146
Issue 1-3
Pages 303-309
ISSN 0167-0115
Publication year 2008
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Institute of Biomedicine, Department of Infectious Medicine
Pages 303-309
Language en
Links dx.doi.org/10.1016/j.regpep.2007.11...
Keywords S5a/Rpn10; Two-yeast hybrid; Lipid raft; Dot blot; Immunofluorescence
Subject categories Cell and Molecular Biology, Microbiology in the medical area

Abstract

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. © 2007 Elsevier B.V. All rights reserved. Keywords: S5a/Rpn10; Two-yeast hybrid; Lipid raft; Dot blot; Immunofluorescence

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