Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 34, Pages 12141-12146Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0504776102
Keywords
seven-transmembrane receptor; signal transduction; ubiquitination; Aspergillus; endocytosis
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- Wellcome Trust Funding Source: Medline
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Metazoan arrestins bind to seven-transmembrane (7TM) receptors to regulate function. Aspergillus nidulans PaIF, a protein involved in the fungal ambient pH signaling pathway, contains arrestin N-terminal and C-terminal domains and binds strongly to two different regions within the C-terminal cytoplasmic tail of the 7TM, putative pH sensor PaIH. Upon exposure to alkaline ambient pH, PaIF is phosphorylated and, like mammalian beta-arrestins, ubiquitinated in a signal-dependent and 7TM protein-dependent manner. Substitution in PaIF of a highly conserved arrestin N-terminal domain Ser residue prevents PaIF-PaIH interaction and pH signaling in vivo. Thus, PalF is the first experimentally documented fungal arrestin-related protein, dispelling the notion that arrestins are restricted to animal proteomes. Epistasis analyses demonstrate that PaIF posttranslational modification is partially dependent on the 4TM protein Pall but independent of the remaining pH signal transduction pathway proteins PaA, PaIB, and PaIC, yielding experimental evidence bearing on the order of participation of the six components of the pH signal transduction pathway. Our data strongly implicate PaIH as an ambient pH sensor, possibly with the cooperation of PaIl.
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