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GenomicsRibosomal protein RPL26 is the principal target of UFMylation
Ribosomal protein RPL26 is the principal target of UFMylation
PRJNA509149 | ENA
ProteomicsLC-MS/MS analysis of ribosome UFMylation in vitro
UFMylation, is a Ubiquitin-like modification occurring on RPL26, a ribosomal subunit, upon ribosome stalling at the ER membrane. This modification is achieved by a pool of enzymes commonly referred to as E1-activating, E2-conjugating and E3-ligase enzymes. The UFM1 E3 ligase comprises of three prote...
ORGANISM(S): Homo sapiens (Human) 
2024-03-22 | PXD046991 | Pride
In vitro reconstitution Rpl26 ufmylation Ribosome ufmylation 
TranscriptomicsRibosomal protein RPL26 is the principal target of UFMylation
UFM1 is a small, metazoan-specific, ubiquitin-like protein modifier that is essential for embryonic development. Although loss-of-function mutations in UFM1 conjugation are linked to ER stress, neither the biological function nor the relevant cellular targets of this protein modifier are known. Here...
ORGANISM(S): Homo sapiens 
2018-12-11 | GSE123539 | GEO
UnknownRibosomal protein RPL26 is the principal target of UFMylation.
Not available
S-EPMC6347690 | biostudies-literature
UnknownUFMylation of RPL26 links translocation-associated quality control to endoplasmic reticulum protein homeostasis.
Not available
S-EPMC6951344 | biostudies-literature
Genomics
RPL26 and gut
PRJNA1312313 | ENA
ProteomicsShuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and C53-mediated autophagy
UFMylation mediates the covalent modification of substrate proteins with UFM1 (Ubiquitin- fold modifier 1) and regulates the selective degradation of endoplasmic reticulum (ER) via autophagy (ER-phagy) to maintain ER homeostasis. Specifically, collisions of the ER-bound ribosomes trigger ribosome UF...
ORGANISM(S): Chlamydomonas reinhardtii 
2022-11-22 | PXD038157 | Pride
Chlamydomonas reinhardtii Rpl26 Er-phagy Ufmylation 
UnknownThe Epstein-Barr virus deubiquitinase BPLF1 regulates stress-induced ribosome UFMylation and reticulophagy.
Not available
S-EPMC12013442 | biostudies-literature
UnknownMechanistic insights into the roles of the UFM1 E3 ligase complex in ufmylation and ribosome-associated protein quality control.
Not available
S-EPMC10438457 | biostudies-literature
UnknownRPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.
Not available
S-EPMC10028864 | biostudies-literature
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