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

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Galindo, Antonio Hervás-Aguilar, América Rodríguez-Galán, Olga Vincent, Olivier Arst, Herbert N. Tilburn, Joan Peñalva, Miguel A.
Description	Country affiliation: Spain Author Affiliation: Galindo A ( Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas CSIC, Ramiro de Maeztu 9, Madrid 28040, Spain.)
Abstract	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, Arg442Delta 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.
File Format	HTM / HTML
ISSN	13989219
e-ISSN	16000854
Journal	Traffic
Issue Number	10
Volume Number	8
Language	English
Publisher	Wiley
Publisher Date	2007-10-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Physiology Aspergillus Nidulans Metabolism Cell Membrane Fungal Proteins Nuclear Proteins Saccharomyces Cerevisiae Proteins Signal Transduction Physiology Amino Acid Sequence Endosomal Sorting Complexes Required For Transport Hydrogen-ion Concentration Molecular Sequence Data Protein Structure, Tertiary Saccharomyces Cerevisiae Transcription Factors Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Genetics Structural Biology Molecular Biology Biochemistry

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