Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth.
作者： Ramona Märker , Bernhard Blank‐Landeshammer , Anna Beier‐Rosberger , Albert Sickmann , Ulrich Kück
DOI: 10.1111/MMI.14475
关键词:
摘要: The highly conserved striatin-interacting phosphatases and kinases (STRIPAK) complex regulates phosphorylation/dephosphorylation of developmental proteins in eukaryotic microorganisms, animals humans. To first identify potential targets STRIPAK, we performed extensive isobaric tags for relative absolute quantification-based proteomic phosphoproteomic analyses the filamentous fungus Sordaria macrospora. In total, identified 4,193 2,489 phosphoproteins, which are represented by 10,635 phosphopeptides. By comparing phosphorylation data from wild type mutants, 228 phosphoproteins to be regulated all three STRIPAK thus representing STRIPAK. provide an exemplarily functional analysis a STRIPAK-dependent phosphorylated protein, selected CLA4, member p21-activated kinase family. Functional characterization ∆cla4 deletion strain showed that CLA4 controls sexual development polarized growth. determine relevance impact specific sites on development, next generated phosphomimetic -deficient variants CLA4. This (de)phosphorylation serine (S685) residue catalytic domain as being important fungal cellular development. Collectively, these significantly contribute understanding mechanistic function phosphatase signaling complex.
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