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

摘要: 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 (Δpro11, Δpro11Δpro22, Δpp2Ac1Δpro22) 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. While S180 was dephosphorylated a STRIPAK-dependent manner, S216, S1343 served non-regulated sites. indistinguishable type, phospho-deficiency S216 resulted drastic reduction growth, 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 microscopy revealed co-localizes endosomal marker shuttles endosomes. new mechanistic model explains how -independent development asexual growth.