{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/LUMOS_YS_20241116.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/LUMOS_YS_20240214.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/LUMOS_YS_20240126.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/LUMOS_YS_20240723.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_05_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_01_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240126_03_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240214_03_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_21_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_17_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240214_01_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240126_01_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_03_ITMSms2hcd.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_19_ITMSms2hcd.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240214_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240126_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240126_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240214_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20241116_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD065356/YS_OrbitrapLUMOS_20240711_19.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["yongshes@uci.edu"],"submitter":["Clinton Yu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Rna degradation","Misprocessed rnas","Rna nuclear retention","Leng8"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065356"],"sample_protocol":["90-minute LC-MS/MS acquisitions were performed on samples acquired from FLAG immunoprecipitation (20241116, 20240723) or RNA pulldown (20240126, 2024021). For FLAG IPs, HEK293T cells were seeded in 10-cm dishes and transfected the next day with pcDNA3 plasmids encoding full-length or truncated LENG8 or GANP. After 48 hours, cells were harvested in cold PBS, centrifuged, and lysed in buffer (20 mM HEPES pH 7.9, 150 mM NaCl, 0.2% NP-40, protease inhibitors). Lysates were sonicated on ice (3 sec on/10 sec off, 6 cycles), cleared by centrifugation, and input samples were collected. For immunoprecipitation, 40 µL FLAG M2 agarose beads were pre-washed; RNase A/T1 was added to specified lysates. Supernatants were incubated with beads at 4 °C for 2 hours. Beads were washed five times and proteins were eluted with FLAG peptide. Eluates were acetone-precipitated at –20 °C overnight, centrifuged, and protein pellets were resuspended in digestion buffer (8 M urea, 25 mM ammonium bicarbonate). For RNA pulldowns, thirty pmol of in vitro-transcribed RNA and 225 pmol of MBP-MS2 fusion protein were incubated in Buffer D-100 (20 mM HEPES pH 7.9, 100 mM NaCl, 1 mM MgCl₂, 0.2 mM EDTA) on ice for 30 minutes to form complexes. ATP, creatine phosphate, yeast tRNA, and HeLa nuclear extract were added, and the volume was adjusted to 1 mL with nuclease-free water. The mixture was incubated at 30°C for 20 minutes, then chilled and centrifuged to remove debris. The supernatant was incubated with 140 µL of amylose resin at 4°C for 1 hour. Beads were washed three times with detergent-containing buffer and once with detergent-free buffer. Proteins were eluted twice using maltose-containing buffer, pooled, and acetone-precipitated overnight at −20°C. The next day, samples were centrifuged, and protein pellets were resuspended in 50 µL of digestion buffer (8 M urea, 25 mM ammonium bicarbonate). Protein eluates were reduced using DTT and alkylated using iodoacetamide prior to tryptic digestion overnight. Following enzymatic digestion, the samples were desalted using Sep-Pak C18 cartridges."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS/MS scans were extracted using PAVA (UCSF) and searched against a random-concatenated SwissProt human proteome database obtained 2024-01-12 using ProteinProspector (v.6.3.5)"],"omics_type":["Proteomics"],"labhead":["Yongsheng Shi"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Microbiology & Molecular Genetics University of California, Irvine Irvine, California, 92697 USA"],"species":["Homo Sapiens (human)"],"publication":["41861815 Tian L, Liu L, Yoon Y, Soles LV, Valdez M, Jeong J, Yu C, Huang L, Shi Y. LENG8 mediates RNA nuclear retention and degradation in eukaryotes. Mol Cell. 2026:S1097-2765(26)00137-1 10.1016/j.molcel.2026.02.023"],"submitter_mail":["clinton.yu@uci.edu"],"submitter_affiliation":["University of California, Irvine"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"LENG8 mediates nuclear retention and degradation of misprocessed mRNAs and noncoding RNAs","description":"Incompletely processed and misprocessed mRNAs as well as numerous noncoding RNAs are retained in the nucleus and often degraded, and defects in this quality control mechanism have been linked to various diseases, including cancer and neurodegeneration. However, the underlying mechanisms remain poorly understood. Here we show that LENG8 is recruited to pre-mRNAs by splicing factors, including the U1 snRNP. Once RNA-bound, LENG8 is both necessary and sufficient to sequester RNA in the nucleus. LENG8 depletion leads to the leakage of misprocessed mRNAs, including intronically polyadenylated and intron-retained mRNAs, as well as noncoding RNAs into the cytoplasm. Mechanistically, we showed that LENG8 binds to PCID2 and SEM1 to form an evolutionarily conserved complex, referred to as REX (repressor of export), and causes RNA nuclear retention by acting as a dominant negative factor for the essential mRNA export factor TREX2. Finally, LENG8 promotes RNA degradation by recruiting the ZFC3H1-MTR4-exosome complex. Thus, LENG8 is a key quality control factor that keeps pre-mRNAs in the nucleus until they are fully and correctly 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