ArticleMolecular plant pathology2018
Fsr1, a striatin homologue, forms an endomembrane-associated complex that regulates virulence in the maize pathogen Fusarium verticillioides.
Article in Molecular plant pathology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- STRIPAK-associated greenbeard proteins DOC1 and DOC2 regulate MAK2 signaling and sexual development in Sordaria macrospora.PLoS biology · 2026Article
- Distinct STRIPAK subunits drive conserved and subunit-specific signaling programs inbioRxiv : the preprint server for biology · 2026Article
- A Core Effector MoPce1 Is Required for the Pathogenicity of Magnaporthe oryzae by Modulating Catalase-Mediated HMolecular plant pathology · 2026Article
- Integrated Proteomic and Metabolomic Profiling of the Secretome ofJournal of fungi (Basel, Switzerland) · 2025Article
- STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024Review
- The Cryptococcus neoformans STRIPAK complex controls genome stability, sexual development, and virulence.PLoS pathogens · 2024Article
- Dual functionality of pathogenesis-related proteins: defensive role in plants versus immunosuppressive role in pathogens.Frontiers in plant science · 2024Article
- The STRIPAK complex orchestrates cell wall integrity signalling to govern the fungal development and virulence of Fusarium graminearum.Molecular plant pathology · 2023Article
- The function of plant PR1 and other members of the CAP protein superfamily in plant-pathogen interactions.Molecular plant pathology · 2023Review
- The STRIPAK component SipC is involved in morphology and cell-fate determination in the nematode-trapping fungus Duddingtonia flagrans.Genetics · 2022Article
- STRIPAK, a Key Regulator of Fungal Development, Operates as a Multifunctional Signaling Hub.Journal of fungi (Basel, Switzerland) · 2021Article
- Two regulators of G-protein signaling (RGS) proteins FlbA1 and FlbA2 differentially regulate fumonisin B1 biosynthesis in Fusarium verticillioides.Current genetics · 2021Article
- ThemSphere · 2021Article
- A Rab GTPase protein FvSec4 is necessary for fumonisin B1 biosynthesis and virulence in Fusarium verticillioides.Current genetics · 2020Article
- Assembly of a heptameric STRIPAK complex is required for coordination of light-dependent multicellular fungal development with secondary metabolism in Aspergillus nidulans.PLoS genetics · 2019Article
- Characterizing co-expression networks underpinning maize stalk rot virulence in Fusarium verticillioides through computational subnetwork module analyses.Scientific reports · 2018Article
- A Cellular Fusion Cascade Regulated by LaeA Is Required for Sclerotial Development inFrontiers in microbiology · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fsr1, a homologue of mammalian striatin, containing multiple protein-binding domains and a coiled-coil (CC) domain, is critical for Fusarium verticillioides virulence. In mammals, striatin interacts with multiple proteins to form a STRIPAK (striatin-interacting phosphatase and kinase) complex that regulates a variety of developmental processes and cellular mechanisms. In this study, we identified the homologue of a key mammalian STRIPAK component STRIP1/2 (striatin-interacting proteins 1 and 2) in F. verticillioides, FvStp1, which interacts with Fsr1 in vivo. Gene deletion analysis indicates that FvStp1 is critical for F. verticillioides stalk rot virulence. In addition, we identified three proteins, designated FvCyp1, FvScp1 and FvSel1, which interact with the Fsr1 CC domain via a yeast two-hybrid screen. Importantly, FvCyp1, FvScp1 and FvSel1 co-localize to endomembrane structures, each having a preferred localization in the cell, and they are all required for F. verticillioides stalk rot virulence. Moreover, these proteins are necessary for the correct localization of Fsr1 to the endoplasmic reticulum (ER) and nuclear envelope. Thus, we identified several novel components in the STRIPAK complex that regulates F. verticillioides virulence, and propose that the correct organization and localization of Fsr1 are critical for STRIPAK complex function.
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