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

ABSTRACT: Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is widely used by eukaryotic cells to control protein fate and cell behaviour¹. 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)^2,3. UFM1 conjugation (UFMylation) facilitates the rescue of 60S ribosomal subunits (60S) that are released after ribosome-associated quality-control-mediated splitting of ribosomes that stall during co-translational translocation of secretory proteins into the ER^3,4. Neither the molecular mechanism by which the UFMylation machinery achieves such precise target selection nor how this ribosomal mod

SUBMITTER: DaRosa PA 

PROVIDER: S-EPMC11469336 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature