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Eisert"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Ubiquitin","Intraflagellar transport","Hedgehog signaling","Flagella","Cilia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062789"],"sample_protocol":["Pulldown with biotinylated polyubiquitin chains (K48- or K63-linked) from cilia/flagella lysates from C. reinhardtii and L. tarentolae.  Flagella were isolated from either C. reinhardtii or L. tarentolae (CC-1690 or P10 strains, respectively).  For K48- or K63- linked pulldowns, 50 µL of Streptavidin agarose beads (Thermo Fisher, #20353) were loaded with 100 µg biotinylated ubiquitin chains in 10 mM Tris-HCl pH 7.4, 150 mM NaCl, 1x protease inhibitor cocktail, and blocked with 10 µM Biotin to block free binding sites, resuspended as a 50% slurry in wash buffer, aliquoted as 100 µl into low-binding 1.5 mL tubes, and incubated with the clarified flagellar lysate rotating end-over-end at 4 °C for 2 h. The beads were then washed four times with 1 mL wash buffer and transferred to a clean 1.5 mL low-binding tube for the final wash. The beads were resuspended in 200 µL elution buffer (10 mM Tris-HCl pH 7.5, 10% SDS) and heated at 70 °C for 10 min to elute protein.   Pulldown with recombinant fusion protein of porcine ARL3-4x(GS)-3xFlag-4x(GS)-CFAP362-342-10His with either wild-type CFAP36 or CFAP36 point mutants immobilized on anti-Flag resin from cilia-enriched porcine trachea isolate.  Cilia was purified from eight fresh porcine trachea (Animal Technologies, Inc.).  Recombinant fusion protein of porcine ARL3-4x(GS)-3xFlag-4x(GS)-CFAP362-342-10His with either wild-type CFAP36 or ubiquitin-binding mutant S163E were immobilized on anti-Flag resin equilibrated in GTP-wash buffer (10 mM Tris pH 7.4, 150 mM NaCl, 1x protease inhibitors, 0.02% NP-40, 100 µM GTP, 200 µM MgCl2) using 60 µg of bait protein and 50 µl of resin per pulldown for 30 min at 22 °C with gentle end-over-end rotation. Lysates of frozen isolated porcine cilia were prepared as described above for L. tarentolae or C. reinhardtii cilia. The resin was washed twice with 1 mL GTP-wash buffer and subsequently incubated with the clarified ciliary lysate for 2 h at 4 °C with gentle end-over-end rotation. Each pulldown was washed four times with 1 mL GTP-wash buffer and the beads transferred to a clean 1.5 mL tube in the final wash step, and eluted with 200 µL elution buffer (10 mM Tris pH 7.4, 10% SDS) and incubated at 70 °C for 10 min to elute protein.  Reductive Alkylation, SP3 Cleanup, digestion, and TMT Labeling Eluants from the pull-downs were treated with 5mM DTT for 1 hour at 37 °C then alkylated with 20mM iodoacetamide with 50mM ammonium bicarbonate for 25min at room temperature in the dark.  The reaction was quenched with 50mM DTT.  Samples were cleaned up following the standard SP3 clean-up protocol.  On bead digestion was performed first by adding 50 µL 200 mM EPPS, pH8.5 with 4% acetonitrile with 1 µL of 2 mg/mL Lys-C (Wako, 129-02541) and shaking at 1000 rpm at 37 °C for 3 hours.  Another 50 µL 200 mM EPPS was added with 1 µL trypsin (Promega, V5113) and digestion continued overnight at 37°C with shaking at 1000 rpm then the digests were transferred to new tubes.  To each digest, 30 µL of LC-MS grade acetonitrile was added and the samples were labeled with either TMTpro or TMT11.  Once labeling was determined to be greater than 95% by LC-SPS-MS3, samples were quenched by adding hydroxylamine to a final concentration of 0.5% V/V for 15 min at room temperature.  The reactions were acidified with formic acid and pooled.  The multiplexes were fractionated by high pH reversed-phase benchtop fractionation (Thermo Scientific, 84868) using the following step gradient of 10%, 12.5%, 15%, 17.5%, 20%, 25%, 30%, 35%, 40%, 50%, 65%, and 80% acetonitrile.  Fractions 1 and 7, 2 and 8, 3 and 9, 4 and 10, 5 and 11, and 6 and 12 were pooled to generate 6 final fractions, which were dried, and desalted by STAGE tip.  LC-MS analysis Data were collected using an Orbitrap Eclipse mass spectrometer pared with a Vanquish Neo UPLC with or without FAIMS.  Peptides were separated on an EASY-Spray PepMap column (Thermo Scientific, ES75750PN) using either a three or four-hour gradient of water to acetonitrile with 0.1% formic acid then analyzed with an SPS-MS3 method.  The high-resolution MS1 spectra were first collected in the orbitrap (resolution 120,000; a scan range of 400-1500; AGC target of 200%, and dynamic exclusion 60sec).  Peptides were fragmented using collision-induced dissociation (CID, CE=35%) and MS2 scans were collected in the ion trap and AGC and maximum injection time set to standard and auto, respectively.  Real-time search and FAIMS were used as indicated with static modifications of alkylated cysteine (+57.0215) and TMTpro or TMT11plex at the N-terminus and lysine sidechains (+304.2071 or +229.162932, respectively) and dynamic modification of oxidized methionine (+15.9949) were permitted.  MS3 precursors were fragmented using high-energy collision-induced dissociation (HCD, CE=50% and 60% for TMTpro and TMT11plex, respectively) then analyzed in the orbitrap with a resolution of 50,000."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The data were analyzed using Gygi Lab GFY Core software.  The raw spectra were converted to mzXML and subsequently post-search calibrated.  Peptide-spectrum matches (PSMs) were made using COMET-based searches (Version 2019.01 rev. 5) with TMT set as a static modification (TMTpro and TMT11 set as +304.2071 and +229.162932, respectively).  Alkylated cysteine was also set as a static modification (+57.02146) and oxidated methionine was set as a dynamic modification (+15.9949).  The protein databases also contained common contaminants and reversed sequences as decoys.  The mass tolerance was set to 20ppm and fragment ion tolerance was set to 1.00.  Using a target-decoy strategy, PSMs were filtered by linear discriminant analysis (LDA) with a false discovery rate (FDR) of 1% and an FDR of 1% for collapsed proteins.  For TMT quantification data were filtered for an isolation specificity above 70% and a minimum summed signal-to-noise of 200 across all TMT channels."],"omics_type":["Proteomics"],"labhead":["Alan Brown"],"instrument_platform":[""],"labhead_affiliation":["Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA."],"submission_type":["COMPLETE"],"species":["Leishmania Tarentolae","Chlamydomonas Reinhardtii","Sus Scrofa Domesticus (domestic Pig)"],"submitter_mail":["robyn_eisert@hms.harvard.edu"],"publication":["40840444 Lange SM, Bennett JA, Eisert RJ, Brown A. A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia. Cell. 2025 188(23):6492-6508.e18 10.1016/j.cell.2025.07.043"],"submitter_affiliation":["Harvard Medical School"],"submitter_country":["United States"],"doi":["10.6019/PXD062789"],"pubmed_abstract":["The temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using a multidisciplinary approach, we demonstrate that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis and demonstrate how structural changes in IFT trains achieve cargo selectivity."],"pubmed_title":["A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia."],"pubmed_authors":["Lange Sven M SM, Bennett Jeremy A JA, Eisert Robyn J RJ, Brown Alan A"],"additional_accession":[]},"is_claimable":false,"name":"A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia","description":"The temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using quantitative proteomics, we identified that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a small GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts Hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis, and demonstrate how structural changes in IFT trains achieve cargo selectivity.","dates":{"publication":"2026-06-29","submission":"2025-04-09"},"accession":"PXD062789","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:222523","NEWT:27602","NEWT: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