title: Conserved Mode of Interaction between Yeast Bro1 Family V Domains and YP(X)nL Motif-Containing Target Proteins.
abstract: Yeast Bro1 and Rim20 belong to a family of proteins which possess a common architecture of Bro1 and V domains. Alix and His domain protein tyrosine phosphatase (HD-PTP), mammalian Bro1 family proteins, bind YP(X)nL (n = 1 to 3) motifs in their target proteins through their V domains. In Alix, the Phe residue, which is located in the hydrophobic groove of the V domain, is critical for binding to the YP(X)nL motif. Although the overall sequences are not highly conserved between mammalian and yeast V domains, we show that the conserved Phe residue in the yeast Bro1 V domain is important for binding to its YP(X)nL-containing target protein, Rfu1. Furthermore, we show that Rim20 binds to its target protein Rim101 through the interaction between the V domain of Rim20 and the YPIKL motif of Rim101. The mutation of either the critical Phe residue in the Rim20 V domain or the YPIKL motif of Rim101 affected the Rim20-mediated processing of Rim101. These results suggest that the interactions between V domains and YP(X)nL motif-containing proteins are conserved from yeast to mammalian cells. Moreover, the specificities of each V domain to their target protein suggest that unidentified elements determine the binding specificity.
authors.affiliation: Department of Agriculture, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, Japan Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan kimura.yoko@shizuoka.ac.jp.
authors.forename: Yoko
authors.initials: Y
authors.lastname: Kimura
authors.affiliation: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, Japan.
authors.forename: Mirai
authors.initials: M
authors.lastname: Tanigawa
authors.affiliation: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
authors.forename: Junko
authors.initials: J
authors.lastname: Kawawaki
authors.affiliation: Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Hyogo, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Takagi
authors.affiliation: Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Hyogo, Japan.
authors.forename: Tsunehiro
authors.initials: T
authors.lastname: Mizushima
authors.affiliation: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, Japan.
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Maeda
authors.affiliation: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
authors.forename: Keiji
authors.initials: K
authors.lastname: Tanaka
mesh_terms: D020816:Amino Acid Motifs / Q000235:genetics*; D000595:Amino Acid Sequence; D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: C480237:Bro1 protein, S cerevisiae; D056827:Endosomal Sorting Complexes Required for Transport; C489601:RIM101 protein, S cerevisiae; D012097:Repressor Proteins; C542553:Rfu1 protein, S cerevisiae; C510979:Rim20 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D017027:Protein Tyrosine Phosphatases