About: BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon

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About: BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon
Creator	Burrone, Oscar Myers, Michael Cesaratto, Francesca Petris, Gianluca Re, Angela Sasset, Linda
Source	PMC
abstract	Translational stalling of ribosome bound to endoplasmic reticulum (ER) membrane requires an accurate clearance of the associated polypeptides, which is not completely understood in mammals. We characterized in mammalian cells the model of ribosomal stalling at the STOP-codon based on proteins tagged at the C-terminus with the picornavirus 2A peptide followed by a termination codon instead of the Proline (2A). We exploited the 2A stalling model to characterize the pathway of degradation of ER-targeted polypeptides. We report that the ER chaperone BiP/GRP78 is a new main factor involved. Moreover, degradation of the ER-stalled polypeptides required the activities of the AAA-ATPase VCP/p97, its associated deubiquitinylase YOD1, the ribosome-associated ubiquitin ligase Listerin and the proteasome. In human proteome, we found two human C-terminal amino acid sequences that cause similar stalling at the STOP-codon. Our data suggest that translational stalling at the ER membrane activates protein degradation at the interface of ribosomal- and ER-associated quality control systems.
has issue date	2019-01-18(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2018.10.009
bibo:pmid	30367842
has license	no-cc
schema:url	https://doi.org/10.1016/j.jmb.2018.10.009
resource representing a document's title	BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon
has PubMed Central identifier	PMC7094721
has PubMed identifier	30367842
schema:publication	J Mol Biol
resource representing a document's body	covid:PMC7094721#body_text
is schema:about of	named entity 'Produced' named entity 'ERAD' named entity 'Membrane-Bound' named entity 'Stalled' named entity 'ERAD' named entity 'biotin' named entity 'mRNAs' named entity 'Ltn' named entity 'protein' named entity 'peptide' named entity 'polypeptides' named entity 'IgG antibody' named entity 'cellular localization' named entity 'interactome' named entity 'polypeptide' named entity 'STOP-codon' named entity 'Fluka' named entity 'peptides' named entity 'methionine' named entity 'secondary antibody' named entity 'C-terminal' named entity 'peptides' named entity 'DNaseI' named entity 'fetal calf serum' named entity 'ubiquitin ligases' named entity 'substrates' named entity 'cycloheximide' named entity 'Cdc48' named entity 'conformation' named entity 'EGFP' named entity 'substrates' named entity 'quality control' named entity '30 mM' named entity 'ubiquitin-proteasome' named entity 'C-termini' named entity 'polypeptides' named entity 'mRNAs' named entity 'mRNAs' named entity 'codon' named entity 'tRNA' named entity 'qRT-PCR' named entity 'inhibitory activity' named entity 'DNA plasmids' named entity 'ENSEMBL' named entity 'ribosome' named entity 'ERAD' named entity 'NGD' named entity 'ERAD' named entity 'coding sequence' named entity 'polypeptides' named entity 'image processing' named entity 'mass spectrometry' named entity 'STOP-codon' named entity 'BiP' named entity 'translation initiation' named entity 'NP-40' named entity 'STOP-codon' named entity 'coding sequences' named entity 'testis' named entity 'Gly' named entity 'GRP78' named entity 'National Institutes of Health' named entity 'ribosome' named entity 'cytosolic' named entity 'Western blot' named entity 'acetic acid' named entity 'protein' named entity 'transfection' named entity 'Listerin' named entity 'cytosolic' named entity 'mammalian cells' named entity 'C-terminal' named entity 'MHC' named entity 'tRNA' named entity 'transfection' named entity 'quality control' named entity 'nucleotide sequence'

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