The STRIPAK signaling complex regulates phosphorylation of GUL1, an RNA-binding protein that shuttles on endosomes

摘要: Abstract The striatin-interacting phosphatase and kinase (STRIPAK) multi-subunit signaling complex is highly conserved within eukaryotes. In fungi, STRIPAK controls multicellular development, morphogenesis, pathogenicity, cell-cell recognition, while in humans, certain diseases are related to this complex. To date, phosphorylation dephosphorylation targets of still widely unknown microbial as well animal systems. Here, we provide an extended global proteome phosphoproteome study using the wild type single double deletion mutants from filamentous fungus Sordaria macrospora. Notably, mutants, identified differential 129 proteins, which 70 sites were previously unknown. Included list eight proteins with RNA recognition motifs (RRMs) including GUL1. Knockout complemented transformants clearly show that GUL1 affects hyphal growth sexual development. assess role on fungal constructed phospho-mimetic -deficient residues S180, S216, S1343. While S1343 indistinguishable wildtype, phospho-deficiency S180 S216 resulted a drastic reduction also fertility. These results thus suggest regulates developmental processes such fruiting body maturation morphogenesis. Moreover, genetic interaction studies strong evidence not integral subunit STRIPAK. Finally, fluorescence microcopy revealed co-localizes endosomal marker shuttles endosomes. new mechanistic model explains how STRIPAK-dependent - independent development asexual growth. Author Summary eukaryotes, variety processes, lack subunits associated severe defects diseases. However, animals, microbes, largely macrospora well-established system used function STRIPAK, since collection experimentally accessible. We established isobaric tag for relative absolute quantification (iTRAQ)-based proteomic phosphoproteomic analysis identify investigate one or two subunits. Our identification putative GUL1, homolog RNA-binding protein SSD1 yeast. Using microscopy, demonstrate investigated deletion, phospho-mimetic, -deletion phosphorylation-dependent manner. Collectively, our comprehensive cellular provides fundamental insights into mechanism target, multiple functions.