Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.ppat.1003527
Title: The Late Endosomal HOPS Complex Anchors Active G-Protein Signaling Essential for Pathogenesis in Magnaporthe oryzae
Authors: Ramanujam R.
Calvert M.E.
Selvaraj P.
Naqvi N.I. 
Keywords: adenylate cyclase
alpha tubulin
cyclic AMP
guanine nucleotide binding protein
phosphatidylinositol 3 phosphate
plasmid vector
RGS protein
scaffold protein
adenylate cyclase
fungal protein
guanine nucleotide binding protein
polyphosphoinositide
article
cell growth
cellular distribution
controlled study
DNA sequence
endosome
fluorescence
immunoprecipitation
Magnaporthe oryzae
microtubule
nonhuman
pathogenesis
pathogenicity
plant leaf
polymerase chain reaction
protein expression
protein localization
protein targeting
seedling
sequence analysis
Southern blotting
genetics
Magnaporthe
metabolism
physiology
signal transduction
Adenylate Cyclase
Fungal Proteins
GTP-Binding Proteins
Magnaporthe
Phosphatidylinositol Phosphates
Signal Transduction
Issue Date: 2013
Publisher: Public Library of Science
Citation: Ramanujam R., Calvert M.E., Selvaraj P., Naqvi N.I. (2013). The Late Endosomal HOPS Complex Anchors Active G-Protein Signaling Essential for Pathogenesis in Magnaporthe oryzae. PLoS Pathogens 9 (8) : e1003527. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.ppat.1003527
Abstract: In Magnaporthe oryzae, the causal ascomycete of the devastating rice blast disease, the conidial germ tube tip must sense and respond to a wide array of requisite cues from the host in order to switch from polarized to isotropic growth, ultimately forming the dome-shaped infection cell known as the appressorium. Although the role for G-protein mediated Cyclic AMP signaling in appressorium formation was first identified almost two decades ago, little is known about the spatio-temporal dynamics of the cascade and how the signal is transmitted through the intracellular network during cell growth and morphogenesis. In this study, we demonstrate that the late endosomal compartments, comprising of a PI3P-rich (Phosphatidylinositol 3-phosphate) highly dynamic tubulo-vesicular network, scaffold active MagA/G?S, Rgs1 (a GAP for MagA), Adenylate cyclase and Pth11 (a non-canonical GPCR) in the likely absence of AKAP-like anchors during early pathogenic development in M. oryzae. Loss of HOPS component Vps39 and consequently the late endosomal function caused a disruption of adenylate cyclase localization, cAMP signaling and appressorium formation. Remarkably, exogenous cAMP rescued the appressorium formation defects associated with VPS39 deletion in M. oryzae. We propose that sequestration of key G-protein signaling components on dynamic late endosomes and/or endolysosomes, provides an effective molecular means to compartmentalize and control the spatio-temporal activation and rapid downregulation (likely via vacuolar degradation) of cAMP signaling amidst changing cellular geometry during pathogenic development in M. oryzae. © 2013 Ramanujam et al.
Source Title: PLoS Pathogens
URI: https://scholarbank.nus.edu.sg/handle/10635/165403
ISSN: 15537366
DOI: 10.1371/journal.ppat.1003527
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