Intra-membrane client recognition potentiates the chaperone functions of Calnexin

ABSTRACT: One third of the human proteome is comprised of membrane proteins, which are particularly vulnerable to misfolding and often require folding assistance by molecular chaperones. Calnexin (CNX), which engages client proteins via its sugar-binding lectin domain, is one of the most abundant ER chaperones, and plays an important role in membrane protein biogenesis. Based on mass spectrometric analyses, we here show that calnexin interacts with a large number of non-glycosylated membrane proteins, indicative of additional non-lectin binding modes. We find that calnexin preferentially bind misfolded membrane proteins, and that it uses its single transmembrane domain (TMD) for client recognition. Combining experimental and computational approaches, we systematically dissect signatures for intramem

SUBMITTER: Dr. Nicolas Bloemeke 

PROVIDER: S-SCDT-10_15252-EMBJ_2022110959 | biostudies-other |

REPOSITORIES: biostudies-other