The covalent conjugation of ubiquitin family proteins is a widespread post-translational protein modification. In the ubiquitin family, the ATG8 subfamily is exceptional because it is conjugated mainly to phospholipids. However, it remains unknown whether other ubiquitin family proteins are also conjugated to phospholipids. Here, we report that ubiquitin is conjugated to phospholipids, mainly phosphatidylethanolamine (PE), in yeast and mammalian cells. Ubiquitinated PE (Ub-PE) accumulates at endosomes and the vacuole (or lysosomes), and its level increases during starvation. Ub-PE is also found in baculoviruses. In yeast, PE ubiquitination is catalyzed by the canonical ubiquitin system enzymes Uba1 (E1), Ubc4/5 (E2), and Tul1 (E3) and is reversed by Doa4. Liposomes containing Ub-PE recruit the ESCRT components Vps27-Hse1 and Vps23 in vitro. Ubiquitin-like NEDD8 and ISG15 are also conjugated to phospholipids. These findings suggest that the conjugation to membrane phospholipids is not specific to ATG8 but is a general feature of the ubiquitin family.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.molcel.2022.08.008 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Emerging Roles of TRIM56 in Antiviral Innate Immunity.
Viruses
January 2025
Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
The tripartite-motif protein 56 (TRIM56) is a RING-type E3 ubiquitin ligase whose functions were recently beginning to be unveiled. While the physiological role(s) of TRIM56 remains unclear, emerging evidence suggests this protein participates in host innate defense mechanisms that guard against viral infections. Interestingly, TRIM56 has been shown to pose a barrier to viruses of distinct families by utilizing its different domains.
View Article and Find Full Text PDFFunctional Characterization of OsCSN1 in the Agronomic Trait Control of Rice Seedlings Under Far-Red Light.
Int J Mol Sci
January 2025
College of Life Sciences, Jilin Agricultural University, Changchun 130118, China.
The COP9 signalosome (CSN) is a highly conserved multi-subunit protein complex, with CSN1 being its largest and most conserved subunit. The N-terminal function of CSN1 plays a pivotal and intricate role in plant photomorphogenesis and seedling development. Moreover, CSN is essential for far-red light-mediated photomorphogenesis in seedlings, but the function of OsCSN1 in seedling growth and development under far-red light conditions has not been determined.
View Article and Find Full Text PDFSystematic Analysis of UFMylation Family Genes in Tissues of Mice with Metabolic Dysfunction-Associated Steatotic Liver Disease.
Genes (Basel)
December 2024
Zhejiang Key Laboratory of Medical Epigenetics, Department of Cell Biology and Genetics, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Background/objectives: UFMylation, a newly identified ubiquitin-like modification, modulates a variety of physiological processes, including endoplasmic reticulum homeostasis maintenance, DNA damage response, embryonic development, and tumor progression. Recent reports showed that UFMylation plays a protective role in preventing liver steatosis and fibrosis, serving as a defender of liver homeostasis in the development of metabolic dysfunction-associated steatotic liver disease (MASLD). However, the regulation of UFMylation in MASLD remains unclear.
View Article and Find Full Text PDFUbiquitination Enzymes in Cancer, Cancer Immune Evasion, and Potential Therapeutic Opportunities.
Cells
January 2025
College of Health and Life Sciences, Hamad Bin Khalifa University, Doha P.O. Box 34110, Qatar.
Ubiquitination is cells' second most abundant posttranslational protein modification after phosphorylation. The ubiquitin-proteasome system (UPS) is critical in maintaining essential life processes such as cell cycle control, DNA damage repair, and apoptosis. Mutations in ubiquitination pathway genes are strongly linked to the development and spread of multiple cancers since several of the UPS family members possess oncogenic or tumor suppressor activities.
View Article and Find Full Text PDFBioinformatics analysis and alternative polyadenylation in Heat Shock Proteins 70 (HSP70) family members.
Int J Physiol Pathophysiol Pharmacol
December 2024
Gene Expression and Signaling Lab, Department of Zoology, Mahatma Gandhi Central University Motihari Motihari, Bihar 845401, India.
Objective: The Heat Shock Protein 70 (HSP70) family is a highly conserved group of molecular chaperones essential for maintaining cellular homeostasis. These proteins are necessary for protein folding, assembly, and degradation and involve cell recovery from stress conditions. HSP70 proteins are upregulated in response to heat shock, oxidative stress, and pathogenic infections.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!