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

19 pages, 9 figures.-- et al.

Detalles Bibliográficos
Autores: Galindo, Antonio, Hervás-Aguilar, América, Rodríguez-Galán, Olga, Vincent, Olivier, Peñalva, Miguel Ángel
Tipo de recurso: artículo
Fecha de publicación:2007
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/24766
Acceso en línea:http://hdl.handle.net/10261/24766
Access Level:acceso abierto
Palabra clave:Arrestin
Aspergillus
Endosomes
ESCRT-III
pH regulation
Signal transduction
7-TMD
id ES_c4da16c3042f9aa2eda2ae24e4b7e1cd
oai_identifier_str oai:digital.csic.es:10261/24766
network_acronym_str ES
network_name_str España
repository_id_str
spelling PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32Galindo, AntonioHervás-Aguilar, AméricaRodríguez-Galán, OlgaVincent, OlivierPeñalva, Miguel ÁngelArrestinAspergillusEndosomesESCRT-IIIpH regulationSignal transduction7-TMD19 pages, 9 figures.-- et al.PalC, 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.A. G. and O. R.-G. were holders of Programa de Formación de Personal Investigador fellowships and O. V. was Ramón y Cajal fellow of the Spanish Ministry of Education and Science. This work was supported by CICYT grants BIO2003-0077 and BIO2006-0556 to M. A. P. and Wellcome Trust grant 067878 to H. N. A. and J. T.Peer reviewedWiley-Blackwell201020102007info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_65011220329 bytesapplication/pdfhttp://hdl.handle.net/10261/24766reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/j.1600-0854.2007.00620.xinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/247662026-05-22T06:33:51Z
dc.title.none.fl_str_mv PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
title PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
spellingShingle PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
Galindo, Antonio
Arrestin
Aspergillus
Endosomes
ESCRT-III
pH regulation
Signal transduction
7-TMD
title_short PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
title_full PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
title_fullStr PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
title_full_unstemmed PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
title_sort PalC, one of two Bro1 domain proteins in the fungal pH signalling pathway, localizes to cortical structures and binds Vps32
dc.creator.none.fl_str_mv Galindo, Antonio
Hervás-Aguilar, América
Rodríguez-Galán, Olga
Vincent, Olivier
Peñalva, Miguel Ángel
author Galindo, Antonio
author_facet Galindo, Antonio
Hervás-Aguilar, América
Rodríguez-Galán, Olga
Vincent, Olivier
Peñalva, Miguel Ángel
author_role author
author2 Hervás-Aguilar, América
Rodríguez-Galán, Olga
Vincent, Olivier
Peñalva, Miguel Ángel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Arrestin
Aspergillus
Endosomes
ESCRT-III
pH regulation
Signal transduction
7-TMD
topic Arrestin
Aspergillus
Endosomes
ESCRT-III
pH regulation
Signal transduction
7-TMD
description 19 pages, 9 figures.-- et al.
publishDate 2007
dc.date.none.fl_str_mv 2007
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/24766
url http://hdl.handle.net/10261/24766
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/j.1600-0854.2007.00620.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1220329 bytes
application/pdf
dc.publisher.none.fl_str_mv Wiley-Blackwell
publisher.none.fl_str_mv Wiley-Blackwell
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869418938014629889
score 15,811543

Similares en LA Referencia