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Submitted on July 1, 2004
Institut für Genetik, Forschungszentrum Karlsruhe, Karlsruhe 76021
Corresponding Author: peter.uetz{at}itg.fzk.de
The phox homology (PX) domain is a phosphoinositide-binding domain that is conserved from yeast to man. Here we show for the first time by genome-wide two-hybrid screens and in vitro binding assays that the PX domain is a bona fide protein interaction domain. The yeast PX domain-only proteins Grd19p (YOR357C) and Ypt35p (YHR105W), as well as the isolated PX domains from Mvp1p (YMR004W), Snx42p/Cvt20p/Atg20p (YDL113C), Vam7p (YGL212W), and Vps17p (YOR132W) yielded a total of 40 reproducible two-hybrid interactions. 35 interactions were found for the full-length proteins of Bem1p (YBR200W), Snx42p, Snx4p/Cvt13p (YJL036W), Vam7p, Vps5p (YOR069W), and Vps17p, but these appear not to require the PX domain, since these interactions could not be reproduced with PX-only baits. Interactions of Grd19p, Vam7p, Vps5p, Vps17p, and Ypt35p with members of the Yip1p family of proteins were detected consistently and were verified by in vitro binding assays. The N-terminal cytoplasmic domain of Yip1p and Yif1p mediates these interactions with PX domains. A mutation in the lipid-binding pocket of Ypt35p that reduces lipid-binding markedly does not affect these PX domain protein interactions, arguing that lipid binding uses a different interaction surface than protein binding.
Revised on July 19, 2004
Accepted on July 19, 2004
The PX domain protein interaction network in yeast
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