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Samples were cooled and loaded onto a 10% Bis-Tris Criterion XT Precast Gel (BioRad #345-0111). SDS-PAGE was performed at 125 V for 120 minutes. The gels were then stained with InstantBlue Coomassie stain (AbCam #ab119211), imaged, and cut in bands. An in-gel digestion was performed after reduction with 2 mM triscarboxyethylphosphine (TCEP) and alkylation with 20 mM iodoacetamide (IAA) followed by digestion with 200 ng of trypsin overnight at 37 °C. Another aliquot of 200 ng trypsin was added the next day for an additional 2-hour digest. Peptides were extracted from the gel pieces using aqueous 50% acetonitrile, containing 0.1% trifluoroacetic acid, then dried down in a vacuum centrifuge. Peptides were resuspended in 200 L of 0.1% trifluoroacetic acid for C18 desalting using a SOLAu plate (Thermo #60209-001), according to the manufacturer’s instructions.  Total eluted, desalted peptides were quantified via a peptide concentration assay (Pierce #23275). 100 ng of peptide were vacuum centrifuged to dryness and resuspended in 30 L of aqueous 0.1% trifluoroacetic acid, then loaded on EvoSep EvoTip Pure tips in preparation for LC-MS/MS analysis. A nanoflow ultra high performance liquid chromatograph and nanoelectrospray orbitrap mass spectrometer (EvoSep and Q Exactive Plus) were used for liquid chromatography-tandem mass spectrometry peptide sequencing (LC-MS/MS).  The sample was loaded onto a EvoTip pure (EV2013), as described above. Trapped peptides were eluted onto the analytical column (EV1106, 15 cm length x 150 µm ID, 1.9 µm particle size).  A factory defined extended gradient (88-minute) was used with solvent A (water + 0.1% formic acid) and solvent B (acetonitrile + 0.1% formic acid). Spray voltage was 1900 V. Capillary temperature was 275 °C. S lens RF level was set at 50. Data-dependent acquisition was performed using Top16 precursors. The mass resolution for MS and MS/MS were set at 70,000 and 17,500 respectively. Dynamic exclusion was set to 15 seconds for previously sampled peaks. Parallel reaction monitoring mass spectrometry was performed for relative quantification of the following peptides: ATG13:  IYFGEVQLSGLGEGFQTVR (3+) and ASPHDVLETIFVR (3+) RBCC1:  EScamCQSTVHQQDETTIDTK (3+) and IQDNNENYQVGLAELR (2+) ULK1:  QLLLALLQR (2+), MFSAGPTGSASSSAR (2+),  and ALLLLEGLQHMLSDQADIENVTK (3+) ULK3:  ASVENLLTEIEILK (2+) and DQEGDSAAALSLYcamK (2+) camC indicates carbamidomethylation of cysteine.  Settings for PRM included: 2.0 m/z isolation windows with no offset, AGC 2e5, Max IT 500 ms, and NCE 28; data were acquired without scheduling.  Kiah Bowers and Bin Fang supported this project."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw files were loaded into Proteome Discoverer 3.0 for database searching with Mascot and Sequest. Database searches were performed against human entries in the UniProt database downloaded 2023_03. Enzyme specificity was set to Trypsin, allowing up to 2 missed cleavages per peptide,  precursor mass tolerance of 10 ppm and fragment mass tolerance of 0.05 Da.  Variable modifications included carbamidomethylation of cysteine and oxidation of methionine. Scaffold 5.0 and Skyline version 23.1 were used to visualize the data.   Mascot results are uploaded here."],"omics_type":["Proteomics"],"labhead":["Conor Lynch"],"instrument_platform":[""],"labhead_affiliation":["Tumor Microenvironment & Metastasis Department Cancer Biology & Evolution Program Moffitt Cancer Center Tampa, FL, USA"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["john.koomen@moffitt.org"],"publication":["Not available"],"submitter_affiliation":["Moffitt Cancer Center"],"submitter_country":["United States"],"doi":["10.6019/PXD067362"],"additional_accession":[]},"is_claimable":false,"name":"Unc-51 Like Kinase 3 (ULK3) is essential for autophagy and cell survival in multiple myeloma","description":"Despite the availability of effective therapies such as proteasome inhibitors, multiple myeloma (MM) patients relapse with refractory disease. To identify new therapeutic targets, we assessed RNA sequencing data from CD138+ MM patient cells (n = 813) across disease stages and found that an autophagy gene signature, and particularly ULK3 expression, was strongly associated with disease progression. Functional studies revealed that ULK3 contributes to MM cell survival as part of the ULK-ATG13-FIP200 complex. We generated inhibitors (SG3-014/MA9-060) with nanomolar potency and confirmed their binding mode through co-crystallization with ULK3. In vivo, ULK3 inhibition reduced MM burden, improved survival, and protected against cancer-induced bone disease. MA9-060 also restored sensitivity to proteasome inhibitors in resistant MM cells. This synergy was validated ex vivo in patient samples, especially those with high ULK3 expression. These findings indicate a new role for ULK3-mediated autophagy in cancer and suggest that ULK3 inhibition is an effective treatment strategy for both newly diagnosed and refractory MM 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