Ontology highlight
ABSTRACT:
SUBMITTER: Meier S
PROVIDER: S-EPMC6739322 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Meier Susanne S Bohnacker Sina S Klose Carolin J CJ Lopez Abraham A Choe Christian A CA Schmid Philipp W N PWN Bloemeke Nicolas N Rührnößl Florian F Haslbeck Martin M Bieren Julia Esser-von JE Sattler Michael M Huang Po-Ssu PS Feige Matthias J MJ
Nature communications 20190911 1
The functionality of most secreted proteins depends on their assembly into a defined quaternary structure. Despite this, it remains unclear how cells discriminate unassembled proteins en route to the native state from misfolded ones that need to be degraded. Here we show how chaperones can regulate and control assembly of heterodimeric proteins, using interleukin 23 (IL-23) as a model. We find that the IL-23 α-subunit remains partially unstructured until assembly with its β-subunit occurs and id ...[more]