title: Novel interaction partners of Bardet-Biedl syndrome proteins.
abstract: Bardet-Biedl syndrome (BBS) is a rare, developmental disorder characterized by six major symptoms: rod-cone dystrophy, obesity, polydactyly, renal abnormalities, learning difficulties, and hypogonadism. Secondary features include cardiac and hepatic anomalies, metabolic disturbancies, and hearing loss. BBS is genetically heterogeneous with 12 disease genes (BBS1-BBS12) described thus far. Current data suggest a functional disturbance in ciliary function and intraflagellar transport being associated with the phenotype. However, the precise functions of the BBS proteins have yet to be elucidated. This study focuses on the detection of protein factors interacting with BBS proteins. Applying yeast two-hybrid (Y2H) technology we found a series of novel, functionally potentially plausible binding partners of BBS1, BBS2, BBS4, and BBS7. Protein interactions were supported by coimmunoprecipitation analyses (ALDOB, EPAS1) and substantiated by colocalization studies at the subcellular level (ALDOB, EXOC7, FLOT1, KRT18, PAX2). Our work provides new insights into the understanding of BBS interactions and thus their biological function.
authors.affiliation: Center of Human Genetics, University of Marburg, 35037 Marburg, Germany. oeffner@staff.uni-marburg.de
authors.forename: F
authors.initials: F
authors.lastname: Oeffner
authors.forename: C
authors.initials: C
authors.lastname: Moch
authors.forename: A
authors.initials: A
authors.lastname: Neundorf
authors.forename: J
authors.initials: J
authors.lastname: Hofmann
authors.forename: M
authors.initials: M
authors.lastname: Koch
authors.forename: K H
authors.initials: KH
authors.lastname: Grzeschik
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D020788:Bardet-Biedl Syndrome / Q000235:genetics / Q000378:metabolism*; D051792:Basic Helix-Loop-Helix Proteins / Q000378:metabolism; D018385:Centrosome / Q000378:metabolism*; D002923:Cilia / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D053538:Keratin-18 / Q000378:metabolism; D007668:Kidney / Q000166:cytology; D008565:Membrane Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins; D051762:PAX2 Transcription Factor / Q000378:metabolism; D020648:Peptide Elongation Factor 1 / Q000378:metabolism; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques; D033921:Vesicular Transport Proteins / Q000378:metabolism; D000099162:Endothelial PAS Domain-Containing Protein 1
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D051792:Basic Helix-Loop-Helix Proteins; D003598:Cytoskeletal Proteins; D005634:Fructose-Bisphosphate Aldolase; D053538:Keratin-18; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D051762:PAX2 Transcription Factor; D020648:Peptide Elongation Factor 1; D011506:Proteins; D033921:Vesicular Transport Proteins; D000099162:Endothelial PAS Domain-Containing Protein 1; C429655:BBS4 protein, human; C464790:Bbs1 protein, human; C473309:Bbs2 protein, human; C473308:Bbs7 protein, human; C094814:EEF1A1 protein, human; C488421:KRT18 protein, human; C497318:PAX2 protein, human; C106354:flotillins