Ontology highlight
ABSTRACT:
SUBMITTER: Karamyshev AL
PROVIDER: S-EPMC3931426 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Karamyshev Andrey L AL Patrick Anna E AE Karamysheva Zemfira N ZN Griesemer Dustin S DS Hudson Henry H Tjon-Kon-Sang Sandra S Nilsson IngMarie I Otto Hendrik H Liu Qinghua Q Rospert Sabine S von Heijne Gunnar G Johnson Arthur E AE Thomas Philip J PJ
Cell 20140101 1-2
Misfolded proteins are often cytotoxic, unless cellular systems prevent their accumulation. Data presented here uncover a mechanism by which defects in secretory proteins lead to a dramatic reduction in their mRNAs and protein expression. When mutant signal sequences fail to bind to the signal recognition particle (SRP) at the ribosome exit site, the nascent chain instead contacts Argonaute2 (Ago2), and the mutant mRNAs are specifically degraded. Severity of signal sequence mutations correlated ...[more]