{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/Deuteration_tables_summary.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/FASTA_Complex_I_GABARAP.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/Difference_plots_all_subunits.pdf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/Complex_I_alone.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/RFU.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/Complex_I_GABARAP.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074963/Peptide_search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["rlw@mrc-lmb.cam.ac.uk"],"submitter":["Maxime Bourguet"],"technology_type":["Mass Spectrometry","MSE","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Autophagy; cryo-em; gabarap; hdx-ms; lc3; positive feedback loop; xl-ms","gabarap","xl-ms","hdx-ms","lc3","positive feedback loop","Autophagy","cryo-em"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074963"],"sample_protocol":["HDX experiments were performed as follows: PtdIns3K-C1 was preincubated for 30 min on ice in the absence or presence of GABARAP, and exposed for different deuteration times (3 s on ice, 3, 30, 300 and 3000 s at room temperature) to a 20 mM HEPES pD8, 150 mM NaCl, 0.5 mM TCEP deuterated buffer (D2O, Thermo Scientific, 166300100) to yield solutions that were 2 μM PtdIns3K-C1 alone or in presence of 50 μM of GABARAP in 80% D2O. Triplicated experiments were performed for each timepoint. Exchange reactions were quenched in 2 M guanidine-hydrochloride, 100 mM glycine, formic acid (Fisher Chemical, 10596814), LC-MS grade water (Romil, H949), pH 2.3 (final pH was 2.5). Samples were then flash-frozen in liquid nitrogen after quenching and stored at −80 °C until analysis. Prior to LC-MS analysis, samples were quickly thawed and injected on a HDX Manager coupled to an Acquity UPLC M-Class system (Waters) set at 0.1 °C. Samples were then digested at 15 °C using a 20 mm x 2.0 mm home-made pepsin column (Pepsin from Thermo Scientific, 20343 and hardware from Upchurch Scientific, C130-B) and loaded on a UPLC pre-column (ACQUITY UPLC BEH C18 VanGuard pre-column, 2.1 mm I.D. x 5 mm, 1.7 μM particle diameter, Waters, 186003975) for 2 min at 100 μL/min. Digested peptides were then eluted over 20 min from the pre-column onto an ACQUITY UPLC BEH C18 column (1.0 mm I.D. x 100 mm, 1.7 μM particle diameter, Waters, 186002346) using a 5−43% gradient of Acetonitrile (Romil, H050), 0.1% formic acid. MS data were acquired using a Synapt G2Si-HDMS (Waters) with electrospray ionization, using the data-independent acquisition mode (MSE) over a m/z range of 50–2000 and a 100 fmol/μL Glu-FibrinoPeptide solution was used for lock-mass correction and calibration. The following parameters were used during the acquisition: capillary voltage, 3 kV; sampling cone voltage, 40 V; source temperature, 90°C; desolvation gas, 150°C and 650 L.h−1; scan time, 0.3 s; trap collision energy ramp, 20–45 eV."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptide identification was performed using ProteinLynx Global Server 3.0.1 (PLGS, Waters) with a home-made protein sequence library containing PIK3C3, PIK3R4, ATG14, BECN1, GABARAP, and pepsin sequences, with peptide and fragment tolerances set automatically by PLGS. Peptides were then filtered using HDExaminer 3.4.0 (Trajan Scientific and Medical) with a minimum fragment per amino acid of 0.2, a minimum intensity of 103, a peptide length between 5 and 25 residues, a minimum PLGS score of 6.62, and an MH+ tolerance of 5 ppm. An initial automated spectral processing step was conducted by HDExaminer followed by a manual inspection of individual peptides for sufficient quality where only one charge state per peptide was kept. Deuterium uptakes were not corrected for back-exchange and are reported as relative. HDX-MS results were statistically validated using an in-house program (Archaeopteryx), where significant differences required 0.3 Da, 5%, and p-value of <0.05 (n=3). HDX-MS results were illustrated on the PDB 9TW2 model using PyMOL 2.5.4 (Schrödinger)."],"omics_type":["Proteomics"],"labhead":["Roger Lee Williams"],"instrument_platform":[""],"labhead_affiliation":["MRC - Laboratory of Molecular Biology"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["mbourguet@mrc-lmb.cam.ac.uk"],"publication":["Not available"],"submitter_affiliation":["MRC Laboratory of Molecular Biology"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"A GABARAP−PtdIns3K-C1 positive feedback loop at the heart of the phagophore nucleation","description":"Macroautophagy/autophagy is a cellular process allowing the degradation of intracellular components during starvation. In mammalian cells, autophagosomes can reach over 1000 nm within 30 min after triggering starvation, but how such substantial amounts of membranes can be synthesized within a brief time remains elusive. A protein complex central to the phagophore initiation is the lipid kinase PIK3C3-Complex 1 (PtdIns3K-C1), which produces phosphatidylinositol-3-phosphate (PtdIns3P). PtdIns3P recruits a variety of downstream proteins, among which are the mammalian ATG8 (mATG8) family proteins which are coupled to the lipids of the phagophore. mATG8s were previously suggested to interact with peptides derived from PtdIns3K-C1, but potential functional implications on the full-complex assembly remained unknown. Here we show that recombinant membrane-coupled mATG8s bind to and potently activate PtdIns3K-C1, with GABARAP being the most potent activator among all mATG8s. By a combination of activity assays, cryo-electronic microscopy (cryo-EM), structural mass spectrometry and mutagenesis, we show that GABARAP binds two sites in PtdIns3K-C1 out of the three that were initially proposed based on peptide binding, with one site showing an atypical bipartite interaction with the mATG8. We also confirm both sites are essential for GABARAP to activate PtdIns3K-C1. We propose this activation of PtdIns3K-C1 by GABARAP forms an unexpected positive feedback loop in cells, whereby basal levels of PtdIns3P production by PtdIns3K-C1 indirectly recruit GABARAP, which in turn helps PtdIns3K-C1 produce more PtdIns3P. This mechanism would be central for autophagosome biogenesis, where enlarged membranes need to be synthesized within a brief 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