Arrestin-related proteins mediate pH signaling in fungi.

Abstract:

:Metazoan arrestins bind to seven-transmembrane (7TM) receptors to regulate function. Aspergillus nidulans PalF, 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 PalH. Upon exposure to alkaline ambient pH, PalF is phosphorylated and, like mammalian beta-arrestins, ubiquitinated in a signal-dependent and 7TM protein-dependent manner. Substitution in PalF of a highly conserved arrestin N-terminal domain Ser residue prevents PalF-PalH 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 PalF posttranslational modification is partially dependent on the 4TM protein PalI but independent of the remaining pH signal transduction pathway proteins PalA, PalB, and PalC, yielding experimental evidence bearing on the order of participation of the six components of the pH signal transduction pathway. Our data strongly implicate PalH as an ambient pH sensor, possibly with the cooperation of PalI.

authors

Herranz S,Rodríguez JM,Bussink HJ,Sánchez-Ferrero JC,Arst HN Jr,Peñalva MA,Vincent O

doi

10.1073/pnas.0504776102

keywords:

subject

Has Abstract

pub_date

2005-08-23 00:00:00

pages

12141-6

issue

34

eissn

0027-8424

issn

1091-6490

pii

0504776102

journal_volume

102

pub_type

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