Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Human UFSP1 is an active UFM1-specific protease

ABSTRACT: In order to confirm the translation initiation site of human UFSP1 (UFM1-specific protease 1), we sought to obtain direct evidence using mass spectrometry (MS) for peptide sequencing.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Xianliang Ma

LAB HEAD: Qian Liang

PROVIDER: PXD033083 | Pride | 2022-04-08

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20201103_KI-6.raw	Raw
	2020713_SH1-1.raw	Raw
	search.zip	Other

Items per page:

1 - 3 of 3

Similar Datasets

Identification of UFM1 candidate targets from mouse brain

Project description:Genetic variants that hinder post-translational protein modifications by the ubiquitin-like modifier UFM1 (UFMylation) cause encephalopathies. UFMylation regulates endoplasmic reticulum (ER) homeostasis, but how UFMylation-deficiencies cause selective neurological defects is unknown. In the framework of our studies on two types of UFMylation pathologies, UFM1 loss and expression of a pathogenic UFM1-R81C variant, we conducted a pilot screen for neuronal UFM1 candidate targets in the mouse brain. We used anti-UFM1 antibodies to affinity-purify potentially UFM1-modified proteins from mouse brain and identified them via a gel-based proteomic approach. Apart from free UFM1, UBA5 and UFC1 as major members of the UFMylation machinery were found to be enriched, providing proof-of-concept to our approach. Among the ~300 potentially UFMylated proteins exclusively identified in the anti-UFM1 antibody sample, we found several guanyl-nucleotide exchange factors, including DOCK4 as the most prominent candidate target. While the UFMylation of DOCK4 remains to be established, this candidate is particularly interesting as it is associated with neurodevelopmental delay and microcephaly. Thus, our findings may open a new area of future investigation toward the role UFMylation in neuronal biology and pathology.

2026-01-28 | PXD071267 | Pride

RNA-seq analysis of UFM1 deletion effect on gene expression during the RIG-I antiviral response

Project description:UFM1 is a post-translational modification that regulates protein function during the ER stress response, DNA damage response, and antiviral response. The goal of this experiment was to determine the role of UFM1 in regulating gene expression induced during RIG-I signaling. We found that deletion of UFM1 broadly decreases transcription of some interferon-stimulated genes during activation of antiviral innate immunity. In subsequent experiments, we found that this is due to UFM1/ufmylation regulation of RIG-I interaction with its trafficking protein 14-3-3epsilon.

2022-03-09 | GSE186287 | GEO

The UFM1 System Alleviated Fatty Acid Oxidation and Chondrocyte Senescence via the UFMylation of CAVIN1

Project description:Osteoarthritis (OA) is a widespread age-related joint disease caused by the gradual loss of chondrocyte function along with age. Here, we found that UFMylation modification was lower-leveled in senescent cartilage, mediated chondrocyte senescence and OA phenotypes through targeting CAVIN1, which acted as a stimulator in chondrocyte senescence, mainly through promoting CPT1 expression and activating fatty acid β-oxidation (FAO). Physiologically, FAO was at a very low level in chondrocytes, while the anomalous activation of FAO accelerated chondrocyte senescence. UFMylation of CAVIN1 promoted its binding with TRIP12, leading to ubiquitination degradation. Therefore, UFMylation played a pivotal role in post-translationally modification of CAVIN1. Polymeric micellar nanoparticles (NPs) conjugated with UFM1 improved the stability of UFM1 recombinant protein (UFM1-rp), and extended the retention time of UFM1-rp in the mouse joint cavity. The administration of UFM1 into mouse joints using an advanced NP delivery system is effective in attenuating age-related pathogenesis. Therefore, we uncovered a previously unknown mechanism, UFM1-CAVIN1-CPT1 axis, in the protection of OA progression and constructed a new drug for OA treatment, and have provided important preliminary evidence toward the translation of our findings into clinical usage.

2024-04-22 | GSE264185 | GEO

Identify UFM1 targeted protein

Project description:we want to identify UFM1 target protein in human cells

2019-04-02 | PXD012729 | Pride

Mass spectrometry of PtGtsf1 interacted proteins in Paramecium tetraurelia

Project description:PtGtsf1 was fused with FlagHA and induced to express in Paramecium tetraurelia. The interacted proteins of PtGtsf1 was obtained by immunoprecipitation with anti-HA antibody, followed with mass spectrometry to identify the proteins. Meanwhile, FlagHA without PtGtsf1 was expressed in Paramecium tetraurelia as control and was performed with same procedures as PtGtsf1-FlagHA. By comparing the enrichment of proteins in PtGtsf1-FlagHA and control, the interacted proteins of PtGtsf1 in Paramecium tetraurelia were identified.

2025-05-06 | PXD049029 | Pride

Human UFSP1 is an active protease that regulates UFM1 maturation and UFMylation

Project description:An essential first step in the posttranslational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is reported to be active since the annotated sequence of UFSP1 lacks critical catalytic residues. Nonetheless, efficient UFM1 maturation occurs in cells lacking UFSP2 suggesting the presence of another active protease. We hereby identify UFSP1 translated from a non-canonical start site to be this protease. Cells lacking both UFSPs show complete loss of UFMylation resulting from an absence of mature UFM1. While UFSP2, but not UFSP1, removes UFM1 from the ribosomal subunit RPL26, UFSP1 acts earlier in the pathway to mature UFM1 and cleave a potential auto-inhibitory modification on UFC1, thereby controlling activation of UFMylation. In summary, our studies reveal distinctions in substrate specificity and localization-dependent functions for the two proteases in regulating UFMylation. The present dataset includes Data Independent Acquisition (DIA) quantitative proteomics analysis of knockout cell lines reported in our study. Our analysis of the processed data is presented in Figure-6.

2022-08-22 | PXD035142 | Pride

Ufm1 binding proteins in heart tissues

Project description:We constructed a Tg-Ufm1 mouse expressing 6×His-labeled Ufm1ΔSC. Potential Ufm1-binding proteins are screened for potential Ufm1-binding proteins by performing pull-down experiments on Tg-Ufm1 and NTg (as controls) mice using His-Tag affinity beads.

2023-05-18 | PXD042349 |

LC-MS/MS of co-immunoprecipitation of 3xFLAG-UFM1 from ribosomal pellet in control and upon anisomycin treatment

Project description:Clearance of arrested nascent polypeptides resulting from ribosomal stalling is essential for proteostasis. Stalled endoplasmic reticulum (ER)-bound ribosomes are marked by ubiquitin-fold modifier 1 (UFM1) on large ribosomal subunit protein RPL26, but the precise role of this process in ribosome-associated quality control (RQC) remains poorly understood. To identify proteins associated with UFMylated ribosomes, we isolated ribosomes from HCT116 cells expressing 3xFLAG-UFM1 upon stalling induction with anisomycin and in control conditions and preformed immunoprecipitation of 3xFLAG-UFM1.

2026-03-23 | PXD071028 | Pride

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

Mechanism of 60S ribosomal subunit recognition and UFMylation by the UFM1 E3 ligase complex

Project description:During co-translational translocation at the endoplasmic reticulum (ER), ribosomes can stall and become covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit RPL26 (uL24). This process, known as UFMylation, is mediated by the UFM1 Ribosome E3 Ligase (UREL) complex, comprised of UFL1, UFBP1, and CDK5RAP3. However, the functional consequences of UFMylation and catalytic mechanisms of UREL are unknown. Here, we present crosslinking-mass spectrometry (XL-MS) data of UREL bound to 60S ribosomes.

2024-03-22 | PXD046990 | Pride