Protein-protein interactions of the PX domain family in yeast.
Carolina Vollert, Peter Uetz
Institute of Genetics, Forschungszentrum Karlsruhe, POB 3640, Karlsruhe, 76021, Germany
The phox homology (PX) domain is a phospho-inositide-lipid-binding domain that is conserved from yeast to man. Here we show by genome-wide two-hybrid screens and in vitro binding assays that 9 out of 15 yeast PX proteins interacted with proteins as well. Interactions were found for Bem1 (YBR200W), Grd19p (YOR357C), Mvp1p (YMR004W), Snx4p/Cvt13p (YJL036W), Snx42p/Cvt20p/Atg20p (YDL113C), Vam7p (YGL212W), Vps17p (YOR132W), Vps5p (YOR069W) and Ypt35p (YHR105W). Only the PX-only proteins Grd19p and Ypt35p as well as the isolated PX domains of Mvp1p, Snx42p, Vam7p, and Vps17p yielded a total of 35 reproducible two-hybrid interactions, most of which were detected with Grd19p (12 interactions) and Ypt35p (15 interactions). Interactions with members of the Yip1/Yif1 family of proteins were detected consistently with Grd19p, Snx42p, Vam7p, Vps17p, and Ypt35p and verified by in vitro binding assays. Several interactions were mapped to domains. The biological meaning of these interactions is discussed. Details are available on our web site: http://itgmv1.fzk.de/www/itg/uetz/.
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