Assessing the roles of striatin orthologs in fungal growth, development and virulence

Chih-Li Wang*, W on-Bo Shim, and Brian D. Shaw

Author address: 

Department of Plant Pathology and Microbiology, Program for the Biology of Filamentous Fungi, Texas A&M University, College Station, TX 77843-2132, USA


Proteins of the striatin family contain a caveolin binding domain, a coiled-coil motif, and a calmodulin binding domain in the N-terminus and a W D40 repeat domain in the C-terminus. Three members of the striatin family, striatin, SG2NA and zinedin, have been identified in multicellular animals while filamentous fungi encode only one homolog. In mammals, they are mainly expressed in neuronal somatodendrites and have been characterized as cytosolic and membrane-bound proteins which play roles in signal transduction and vesicular trafficking. The striatin orthologs in filamentous fungi are associated with virulence of maize stalk rot and perithecium development in Fusarium verticillioides (Fvfsr1), and F. graminearum ( Fgfsr1). In Sordaria macrospora, PRO11 is membrane bound and associated with sexual development. W e generated Cgfsr1 deletion mutant in Colletotrichum graminicola, the maize stalk rot and leaf anthracnose pathogen, to characterize its roles. The mutant showed reduced growth and reduced conidiation. The virulence of the mutant will be discussed. Additionally, the fsrA deletion mutant in Aspergillus nidulans also showed restricted colony growth with red pigment accumulation and altered sexual development. The subcellular localization of a fsrA::GFP fusion in Aspergillus nidulans was consistent with localization to the endoplasmic reticulum and the nuclear envelope. The detailed characters of mutants and further experimental identification of the subcellular localization will be disscussed. *Student poster

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Full conference title: 

6th International Aspergillus Meeting
    • Asperfest 6 (2009)