Ubiquitination of phosphatidylethanolamine in organellar membranes. 2022

Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.

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.

UI MeSH Term Description Entries
D008081 Liposomes Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins. Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
D008322 Mammals Warm-blooded vertebrate animals belonging to the class Mammalia, including all that possess hair and suckle their young. Mammalia,Mammal
D010714 Phosphatidylethanolamines Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids. Cephalin,Cephalins,Ethanolamine Phosphoglyceride,Ethanolamine Phosphoglycerides,Ethanolamineglycerophospholipids,Phosphoglyceride, Ethanolamine,Phosphoglycerides, Ethanolamine
D010743 Phospholipids Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. Phosphatides,Phospholipid
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D044763 Ubiquitin-Conjugating Enzymes A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES. Ubiquitin-Conjugating Enzyme,HHR6 Protein,Ubiquitin-Conjugating Enzyme E2,E2, Ubiquitin-Conjugating Enzyme,Enzyme E2, Ubiquitin-Conjugating,Enzyme, Ubiquitin-Conjugating,Enzymes, Ubiquitin-Conjugating,Ubiquitin Conjugating Enzyme,Ubiquitin Conjugating Enzyme E2,Ubiquitin Conjugating Enzymes
D054875 Ubiquitination The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs. Ubiquitylation
D056827 Endosomal Sorting Complexes Required for Transport A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes. ESCRT Complexes,ESCRT I,ESCRT II,ESCRT III,ESCRT Machinery,Endosomal Sorting Complex Required for Transport,Endosomal Sorting Complex Required for Transport I,Endosomal Sorting Complex Required for Transport II,Endosomal Sorting Complex Required for Transport III,Endosomal Sorting Complex Required for Transport Machinery,Complexes, ESCRT,Machinery, ESCRT
D018160 Receptors, Cytoplasmic and Nuclear Intracellular receptors that can be found in the cytoplasm or in the nucleus. They bind to extracellular signaling molecules that migrate through or are transported across the CELL MEMBRANE. Many members of this class of receptors occur in the cytoplasm and are transported to the CELL NUCLEUS upon ligand-binding where they signal via DNA-binding and transcription regulation. Also included in this category are receptors found on INTRACELLULAR MEMBRANES that act via mechanisms similar to CELL SURFACE RECEPTORS. Cytoplasmic Receptor,Cytoplasmic and Nuclear Receptors,Cytosolic and Nuclear Receptors,Hormone Receptors, Cytoplasmic,Hormone Receptors, Nuclear,Nuclear Hormone Receptor,Nuclear Receptor,Nuclear and Cytoplasmic Receptors,Cytoplasmic Hormone Receptors,Cytoplasmic Receptors,Cytosol and Nuclear Receptors,Intracellular Membrane Receptors,Nuclear Hormone Receptors,Nuclear Receptors,Receptors, Cytoplasmic,Receptors, Cytosol and Nuclear,Receptors, Cytosolic and Nuclear,Receptors, Intracellular Membrane,Receptors, Nuclear,Receptors, Nuclear and Cytoplasmic,Hormone Receptor, Nuclear,Membrane Receptors, Intracellular,Receptor, Cytoplasmic,Receptor, Nuclear,Receptor, Nuclear Hormone,Receptors, Cytoplasmic Hormone,Receptors, Nuclear Hormone

Related Publications

Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
May 2011, Cold Spring Harbor protocols,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
February 2006, Molecular & cellular proteomics : MCP,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
May 1981, Biochimica et biophysica acta,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
January 2017, Methods in molecular biology (Clifton, N.J.),
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
August 1982, Journal of lipid research,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
November 2018, Nature communications,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
February 1999, European journal of biochemistry,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
August 2017, The journal of physical chemistry. B,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
September 1971, The Biochemical journal,
Jun-Ichi Sakamaki, and Koji L Ode, and Yoshitaka Kurikawa, and Hiroki R Ueda, and Hayashi Yamamoto, and Noboru Mizushima
May 2009, Biochimica et biophysica acta,
Copied contents to your clipboard!