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UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER

ABSTRACT: Supporting MS data for paper (doi: 10.1038/s41586-024-07073-0) by DaRosa P.A., Penchev I. et al., titled "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER". Index of MS supporting files uploaded: - Related to Fig. 1a and Extended Data Fig. 1a (AO3435-AO3440: TMT proteomics (Unimod: 35; 737; 4)). - Related to Fig. 1b, c (see MSV000093721).

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Alban Ordureau Joao A. Paulo

PROVIDER: MSV000093510 | MassIVE | Mon Nov 27 07:56:00 GMT 2023

REPOSITORIES: MassIVE

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UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER.

DaRosa Paul A PA Penchev Ivan I Gumbin Samantha C SC Scavone Francesco F Wąchalska Magda M Paulo Joao A JA Ordureau Alban A Peter Joshua J JJ Kulathu Yogesh Y Harper J Wade JW Becker Thomas T Beckmann Roland R Kopito Ron R RR

Nature 20240221 8003

Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is widely used by eukaryotic cells to control protein fate and cell behaviour<sup>1</sup>. UFM1 is a UBL that predominantly modifies a single lysine residue on a single ribosomal protein, uL24 (also called RPL26), on ribosomes at the cytoplasmic surface of the endoplasmic reticulum (ER)<sup>2,3</sup>. UFM1 conjugation (UFMylation) facilitates the rescue of 60S ribosomal subunits (60S) that are released aft ...[more]

PMID: 38383785

Similar Datasets

UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER

Project description:Supporting MS data for paper (doi: 10.1038/s41586-024-07073-0) by DaRosa P.A., Penchev I. et al., titled "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER". Index of MS supporting files uploaded: Related to Related to Fig. 1b, c (xb01004(UFM1), xb01005(SBP-UFM1): LFQ IP-MS (Unimod: 35; 4)). See also MSV000093510

2023-12-22 | MSV000093721 | MassIVE

Recycling of autophagosomal components from autolysosomes by the recycler complex

Project description:The autophagic SNARE protein STX17 is recruited to autophagosomes and translocated to autolysosome after fusion of autophagosomes with lysosomes 30-32. We observed that the number of autophagic vacuoles with STX17 significantly increased after 2 hours of starvation. However, the number of STX17 puncta significantly decreased during prolonged starvation of 5 hours (Fig. 1a). Interestingly, no obvious degradation of STX17 was observed after prolonged starvation (Fig. 1b)

2022-01-24 | PXD031183 |

Human cerebrospinal fluid autoantibody lipid microarray profiling

Project description:This SuperSeries is composed of the following subset Series: GSE37664: Human cerebrospinal fluid autoantibody lipid microarray profiling (Fig. 1A) GSE37670: Human cerebrospinal fluid autoantibody lipid microarray profiling (Fig. 2A) GSE37826: Human cerebrospinal fluid autoantibody lipid microarray profiling (Fig. 2C) Refer to individual Series

2012-05-08 | E-GEOD-37830 | biostudies-arrayexpress

Quantitative Proteome Remodeling Characterization of Two Human Reference Pluripotent Stem Cell Lines During Neurogenesis and Cardiomyogenesis

Project description:Supporting raw MS data for paper (doi: 10.1002/pmic.202100246) by Nam K.H. et al, titled "Quantitative Proteome Remodeling Characterization of Two Human Reference Pluripotent Stem Cell Lines During Neurogenesis and Cardiomyogenesis". Index of RAW files uploaded: - Related to Figure 1 (KN97-120: whole proteome (Unimod: 35; 2016; 4)). - Related to Figure 2 (KN121-126: phospho proteome (Unimod: 35; 21; 2016; 4)) - Related to Figures 3 and 4 (KN205-228: whole proteome (Unimod: 35; 2016; 4))

2022-02-14 | MSV000088833 | MassIVE

Hcr1/eIF3j is a 60S ribosomal subunit recycling accessory factor in vivo

Project description:Hcr1/eIF3j is a sub-stoichiometric subunit of eukaryotic initiation factor 3 (eIF3) that can dissociate the post-termination 40S ribosomal subunit from mRNA in vitro. We examined this ribosome recycling role in vivo by ribosome profiling and reporter assays and found that loss of Hcr1 led to reinitiation of translation in 3’UTRs, consistent with a defect in recycling. However, the defect appeared to be in recycling of the 60S subunit, rather than the 40S subunit, because reinitiation did not require an AUG codon and was suppressed by overexpression of the 60S dissociation factor Rli1/ABCE1. Consistent with a 60S recycling role, overexpression of Hcr1 could not compensate for loss of 40S recycling factors Tma64/eIF2D and Tma20/MCT-1. Intriguingly, loss of Hcr1 triggered higher expression of RLI1 via an apparent feedback loop. These findings suggest Hcr1/eIF3j is recruited to ribosomes at stop codons and may coordinate the transition to a new round of translation.

2019-05-23 | GSE124204 | GEO

CTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway

Project description:Supporting raw MS data for paper (doi: 10.1016/j.molcel.2024.04.026) by Yi S.A. et al, titled "CTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway". Index of RAW files uploaded: - Related to Supplementary Table 1 (HA-9-81-X | WT (1), ATG7KO (2), RB1CC1 (3): whole proteome (Unimod: 35; 2016; 4)). - Related to Supplementary Table 2 - Proteome (HA-1-50: whole proteome (Unimod: 35; 2016; 4)). - Related to Supplementary Table 2 - PhosphoSites (HA-1-50_Phos: phospho proteome (Unimod: 35; 21; 2016; 4)) - Related to Supplementary Table 3 (Yis-1-49: whole proteome (Unimod: 35; 2016; 4))

2022-11-29 | MSV000090814 | MassIVE

Sequestration of ribosomal subunits as inactive 80S by targeting eIF6 limits mitotic exit and cancer progression

Project description:Moderating the pool of active ribosomal subunits is critical for maintaining global translation rates. A crucial factor for modulating the 60S ribosomal subunits is eukaryotic translation initiation factor 6. Release of eIF6 from 60S is essential to permit 60S interactions with 40S. Here, using the N106S mutant of eIF6, we show that disrupting eIF6 interaction with 60S leads to an increase in vacant 80S. It further highlights a dichotomy in the anti-association activity of eIF6 that is distinct from its role in 60S biogenesis and shows that the nucleolar localization of eIF6 is not dependent on uL14-BCCIP interactions. Limiting active ribosomal pools markedly deregulates translation especially in mitosis and leads to chromosome segregation defects, mitotic exit delays and mitotic catastrophe. Ribo-Seq analysis of the eIF6-N106S mutant shows a significant downregulation in the translation efficiencies of mitotic factors and specifically transcripts with long 3′UTRs. eIF6-N106S mutation also limits cancer invasion, and this role is correlated with the overexpression of eIF6 only in high-grade invasive cancers suggesting that deregulation of eIF6 is probably not an early event in cancers. Thus, this study highlights the segregation of eIF6 functions and its role in moderating 80S availability for mitotic translation and cancer progression.

2024-12-04 | GSE272516 | GEO

Sequestration of ribosomal subunits as inactive 80S by targeting eIF6 limits mitotic exit and cancer progression

2024-12-04 | GSE272515 | GEO

NAK-associated protein 1/NAP1 activates TBK1 to ensure accurate mitosis and cytokinesis.

Project description:Supporting raw MS data for paper (DOI:10.1083/jcb.202303082) by Paul S. et al., titled "NAK-associated protein 1/NAP1 activates TBK1 to ensure accurate mitosis and cytokinesis". Index of MS supporting files uploaded: - Related to Figure 6A;S4A (AO3556-AO3579: whole proteome (Unimod: 35; 2016; 4)). - Related to Figure 6A-D;S4B-D (AO3580-AO3603: phospho proteome (Unimod: 35; 21; 2016; 4)). TMTpro channel: WT-UT (126, 127n, 127c, 128n), WT-MRT (128c, 129n, 129c, 130n), TBK1_KO-UT (130c, 131n, 131c, 132n), TBK1_KO-MRT (132c, 133n, 133c, 134n).

2023-11-01 | MSV000093220 | MassIVE

Differentially expressed genes in B-1b compared to B-1a

Project description:B-1b cells are known to produce higher IgM level compared to B-1a cells. This study aims to identify differentially expressed genes and pathways that might enrich in B-1b cells and contribute to higher IgM production.

2022-06-30 | GSE207011 | GEO

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