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

ABSTRACT: STRIPAK is a highly conserved eukaryotic signalling complex controlling a wide range of developmental processes in microorganisms as well as humans. This study uses iTRAQ-based proteomic and phosphoproteomic analyses to expand the identification of differentially phosphorylated proteins, comparing the wildtype proteome of the model fungus S. macorspora to those from three STRIPAK single- and double deletion mutants. Among the differentially phosphorylated proteins, we detected Gul1, a homolog of GUL-1 from N. crassa and SSD1 from yeast. In this study, we further provide a functional analysis of Gul1, showing it controls sexual development and hyphal morphology in a phosphorylation dependent manner.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Sordaria Macrospora K-hell

SUBMITTER: Bernhard Blank-Landeshammer

LAB HEAD: Prof. Dr. Albert Sickmann

PROVIDER: PXD021646 | Pride | 2020-09-24

REPOSITORIES: pride

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			Action	DRS
	BB_Sordaria2_iTRAQ_TiO2_HILIC.msf	Msf
	BB_Sordaria2_iTRAQ_pH8.msf	Msf
	QExactiveHF02_03555.raw	Raw
	QExactiveHF02_03556.raw	Raw
	QExactiveHF02_03557.raw	Raw

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The STRIPAK dependent phosphorylation of distinct residues of GUL1 controls hyphal morphology and sexual fertility

Project description:STRIPAK is a highly conserved eukaryotic signalling complex controlling a wide range of developmental processes in microorganisms as well as humans. This study uses iTRAQ-based proteomic and phosphoproteomic analyses to expand the identification of differentially phosphorylated proteins, comparing the wildtype proteome of the model fungus S. macorspora to those from three STRIPAK single- and double deletion mutants. Among the differentially phosphorylated proteins, we detected Gul1, a homolog of GUL-1 from N. crassa and SSD1 from yeast. In this study, we further provide a functional analysis of Gul1, showing it controls sexual development and hyphal morphology in a phosphorylation dependent manner.

2020-09-30 | PXD016296 | Pride

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Project description:Biotin identification (BioID) is a proximity-dependent labeling technique to study protein-protein co-localization in vivo. Although BioID has been applied in animal cells, plants and yeast, the method remained to be established in filamentous fungi. In this study, we established BioID for the filamentous fungus Sordaria macrospora using the well-characterized striatin interacting phosphatase and kinase (STRIPAK) complex as a proof of principle. In detail, the STRIPAK complex interactor 1 (SCI1) was fused to a codon-optimized TurboID biotin ligase. This SCI1-TurboID fusion protein complemented the Δsci1 deletion strain phenotype. The identification of the already known SmSTRIPAK components PRO11, SmMOB3, SmPP2Ac1 and PRO22 in a BioID experiment with SCI1-TurboID demonstrated its successful application in S. macrospora. The technique will provide a powerful proteomics tool for fungal biologists.

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