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Título

PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32

AutorGalindo, Antonio ; Hervás-Aguilar, América ; Rodríguez-Galán, Olga ; Vincent, Olivier ; Peñalva, Miguel Ángel
Palabras claveArrestin
Aspergillus
Endosomes
ESCRT-III
pH regulation
Signal transduction
7-TMD
Fecha de publicaciónoct-2007
EditorWiley-Blackwell
CitaciónTraffic 8(10):1346-1364(2007)
ResumenPalC, distantly related to Saccharomyces cerevisiae peripheral endosomal sorting complexes required for transport III (ESCRT-III) component Bro1p and one of six Aspergillus nidulans pH signalling proteins, contains a Bro1 domain. Green fluorescent protein (GFP)-tagged PalC is recruited to plasma membrane-associated punctate structures upon alkalinization, when pH signalling is active. PalC recruitment to these structures is dependent on the seven transmembrane domain (7-TMD) receptor and likely pH sensor PalH. PalC is a two-hybrid interactor of the ESCRT-III Vps20/Vps32 subcomplex and binds Vps32 directly. This binding is largely impaired by Pro439Phe, Arg442Ala and Arg442His substitutions in a conserved region mediating interaction of Bro1p with Vps32p, but these substitutions do not prevent cortical punctate localization, indicating Vps32 independence. In contrast, Arg442Δ impairs Vps32 binding and prevents PalC-GFP recruitment to cortical structures. pH signalling involves a plasma membrane complex including the 7-TMD receptor PalH and the arrestin-like PalF and an endosomal membrane complex involving the PalB protease, the transcription factor PacC and the Vps32 binding, Bro1-domain-containing protein PalA. PalC, which localizes to cortical structures and can additionally bind a component of ESCRT-III, has the features required to bridge these two entities. A likely S. cerevisiae orthologue of PalC has been identified, providing the basis for a unifying hypothesis of gene regulation by ambient pH in ascomycetes.
Descripción19 pages, 9 figures.-- et al.
Versión del editorhttp://dx.doi.org/10.1111/j.1600-0854.2007.00620.x
URIhttp://hdl.handle.net/10261/24766
DOI10.1111/j.1600-0854.2007.00620.x
ISSN1398-9219
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