Título
Comparative live-cell imaging analyses of SPA-2, BUD-6 and BNI-1 in Neurospora crassa reveal novel features of the filamentous fungal polarisome
Autor
Alexander Lichius
Colaborador
MARIO ENRIQUE YAÑEZ GUTIERREZ (Colaborador)
Nick Read (Colaborador)
Ernestina Castro-Longoria (Colaborador)
Nivel de Acceso
Acceso Abierto
Identificador alterno
doi: https://doi.org/10.1371/journal.pone.0030372
Materias
fungal protein, protein BNI 1, protein BUD 6, protein SPA 2, protein Spk, unclassified drug, actin binding protein, cytoskeleton protein, fungal protein, article, cell fusion, cellular distribution, comparative study, conidium, controlled study, cyto - (SCOPUS) BIOLOGÍA Y QUÍMICA - (CTI) CIENCIAS DE LA VIDA - (CTI) MICROBIOLOGÍA - (CTI) MICROBIOLOGÍA - (CTI)
Resumen o descripción
A key multiprotein complex involved in regulating the actin cytoskeleton and secretory machinery required for polarized growth in fungi, is the polarisome. Recognized core constituents in budding yeast are the proteins Spa2, Pea2, Aip3/Bud6, and the key effector Bni1. Multicellular fungi display a more complex polarized morphogenesis than yeasts, suggesting that the filamentous fungal polarisome might fulfill additional functions. In this study, we compared the subcellular organization and dynamics of the putative polarisome components BUD-6 and BNI-1 with those of the bona fide polarisome marker SPA-2 at various developmental stages of Neurospora crassa. All three proteins exhibited a yeast-like polarisome configuration during polarized germ tube growth, cell fusion, septal pore plugging and tip repolarization. However, the localization patterns of all three proteins showed spatiotemporally distinct characteristics during the establishment of new polar axes, septum formation and cytokinesis, and maintained hyphal tip growth. Most notably, in vegetative hyphal tips BUD-6 accumulated as a subapical cloud excluded from the Spitzenkörper (Spk), whereas BNI-1 and SPA-2 partially colocalized with the Spk and the tip apex. Novel roles during septal plugging and cytokinesis, connected to the reinitiation of tip growth upon physical injury and conidial maturation, were identified for BUD-6 and BNI-1, respectively. Phenotypic analyses of gene deletion mutants revealed additional functions for BUD-6 and BNI-1 in cell fusion regulation, and the maintenance of Spk integrity. Considered together, our findings reveal novel polarisome-independent functions of BUD-6 and BNI-1 in Neurospora, but also suggest that all three proteins cooperate at plugged septal pores, and their complex arrangement within the apical dome of mature hypha might represent a novel aspect of filamentous fungal polarisome architecture. © 2012 Lichius et al.
Editor
Alexandra Carolyn Brand, University of Aberdeen, United Kingdom
Fecha de publicación
2012
Tipo de publicación
Artículo
Versión de la publicación
Versión publicada
Recurso de información
Formato
application/pdf
Fuente
PLoS ONE, Vol.7, No.1, Pags.1-23
Idioma
Inglés
Sugerencia de citación
Lichius A., Yáñez-Gutiérrez M.E., Read N.D., Castro-Longoria E.2012. Comparative Live-Cell Imaging Analyses of SPA-2, BUD-6 and BNI-1 in Neurospora crassa Reveal Novel Features of the Filamentous Fungal Polarisome. PLoS ONE 7(1): e30372. https://doi.org/10.1371/journal.pone.0030372
Repositorio Orígen
Repositorio Institucional CICESE
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