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ProteomicsProximity labeling of the SmSTRIPAK complex in Sordaria macrospora using the SCI1 subunit as bait to identify its SmSTRIPAK-dependent microenvironment
In this study, we used the in vivo proximity labeling biotin identification (BioID; Roux et al., 2012) method to capture proteins of the microenvironment of the striatin interacting kinase and phosphatase complex of the filamentous fungus Sordaria macrospora (SmSTRIPAK). For that, the TurboID biotin...
ORGANISM(S): Sordaria macrospora 
2026-08-19 | PXD069198 | Pride
Sordaria macrospora Turboid Stripak Proximity labeling Bioid 
ProteomicsProxiomes of the greenbeard proteins SmDOC1 and SmDOC2 in the filamentous fungus Sordaria macrospora
In this study, we used the in vivo proximity labeling biotin identification (BioID; Roux et al., 2012) method to capture proteins of the microenvironment of the greenbeard determinant of communication (DOC) proteins SmDOC1 and SmDOC2 in the filamentous fungus Sordaria macrospora. The genes Smdoc1 (S...
ORGANISM(S): Sordaria macrospora 
2026-08-19 | PXD069539 | Pride
Sordaria macrospora Turboid Proximity labeling Bioid Determinant of communication 
ProteomicsLYM2 mediates chitin-induced plasmodesmal flux reduction in Populus x canescens
LYSIN MOTIF DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYL INOSITOL-ANCHORED PROTEIN 2 (LYM2) is a GPI-anchored LysM receptor-like protein (LysM-RLP) that harbors three extracellular LysM-domains and a GPI moiety at the C-terminus. LYM2 in Arabidopsis thaliana is involved in chitin-mediated plasmodesmal flu...
ORGANISM(S): Populus canescens (Grey poplar) (Populus tremula x Populus alba) 
2026-09-07 | PXD058986 | Pride
Plasmodesmal flux Lysm-rlp Alternative splicing Chitin-binding affinity 
ProteomicsFungal COP9 signalosome assembly requires connection of two trimeric intermediates for integration of intrinsic deneddylase
The eight-subunit COP9 signalosome (CSN complex), controls the exchange of E3 ubiquitin cullin RING ligase receptors through its deneddylase activity, providing specificity to eukaryotic protein degradation. The conserved eight-subunit CSN complex is required for multicellular development of the fil...
ORGANISM(S): Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) 
2023-08-10 | PXD043205 | Pride
Cop9 signalosome Aspergillus nidulans Gfp-affinity purifications Csn complex Native complex assembly Subcomplexes 
ProteomicsEstablishment of TurboID proximity proteomics in the filamentous fungus Sordaria macrospora
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 filam...
ORGANISM(S): Sordaria macrospora 
2022-10-25 | PXD034217 | Pride
Sordaria macrospora Turboid Stripak Proximity labeling Bioid 
ProteomicsAsc1p-dependent phosphorylation of Ubp3p-associated Bre5p
The phosphorylation of Bre5p was analyzed in ASC1 wild-type and Δasc1 cells. Bre5p was co-purified from cell extracts with its GFP-tagged interaction partner Ubp3p in GFP-trap experiments. Trapped proteins were in-gel digested with trypsin and analyzed with the Q Exactive HF (Thermo Scientific). Pro...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-10-09 | PXD007858 | Pride
Bre5 Phosphorylation Ubp3 Saccharomyces cerevisiae Asc1/rack1 
ProteomicsPhosphorylation of Asc1p and Asc1p-dependent phospho-proteome
Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome We determined 1) the phosphorylation sites within the Asc1 protein purified from Saccharomyces cerevisiae via its Strep-tag and 2) the Asc1p-dependent phospho-proteome. 1) Phospho-sites within tryptic peptides of Asc1p were identified usi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-12-13 | PXD003031 | Pride
Lc-msms Asc1p Rack1 Silac Signal transduction Phosphorylation Saccharomyces cerevisiae Translation 
ProteomicsIn vivo proximity-labeling with miniTurboID to screen for protein-protein interactions in the filamentous ascomycete Sordaria macrospora
The Biotin Identification (BioID) method is an in vivo labeling strategy for the identification of cellular microenvironments in animal cells, plants, yeast and filamentous fungi. With this method, the protein of interest (POI) is fused to a promiscuous biotin ligase. The ligase biotinylates proxima...
ORGANISM(S): Sordaria macrospora 
2025-05-12 | PXD061752 | Pride
Sordaria macrospora Stripak Proximity labeling Miniturbo Miniturboid Bioid 
ProteomicsA rendezvous of two second messengers: The c-di-AMP receptor protein DarB controls (p)ppGpp synthesis in Bacillus subtilis
DarB is a cyclic di-AMP binding protein consisting of two CBS (Cystathionine-beta synthase) domains. To reveal the global role of the second-messenger, understanding the function of the receptor proteins is fundamental. In order to do so, we aimed to identify potential binding partners of DarB in vi...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2021-01-12 | PXD018087 | Pride
Rela Bacillus subtilis Pull-down Second messengers C-di-amp receptor Darb 
ProteomicsAnalysis of the Putative Nucleoporin POM33 in the Filamentous Fungus Sordaria macrospora
The POM33 protein of Sordaria macrospora is a nucleoporin considered of being an ER-protein that may function in ER-shaping and organization. In this study, we performed TagRFP-T pulldown experiments in S. macrospora strains expressing either POM33-TagRFP-T or the free TagRFP-T as control to identif...
ORGANISM(S): Sordaria macrospora 
2021-08-23 | PXD026253 | Pride
Stripak Sordaria macrospora. pom33 Endoplasmatic reticulum 
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