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ProteomicsIntramembrane client recognition potentiates the chaperone functions of calnexin
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 chaperone...
ORGANISM(S): Homo sapiens (Human) 
2022-11-09 | PXD031140 | Pride
Membrane proteins Protein quality control Molecular chaperones Calnexin 
ProteomicsSelective regulation of aspartyl intramembrane protease activity by calnexin
Signal peptide peptidase-like 2c (SPPL2c) is a testis-specific aspartyl intramembrane protease that contributes to male gamete function both by catalytic and non-proteolytic mechanisms. Here, we provide an unbiased characterisation of the in vivo interactome of SPPL2c identifying the ER chaperone ca...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD052965 | Pride
Co-ip Signal peptide peptidase-like 2c Mouse Calnexin Sppl2c Testis 
ProteomicsCalnexin depletion by ER-stress during cholestasis inhibits the Na+-taurocholate Cotransporting Polypeptide (NTCP)
Impaired bile flow (cholestasis) leads to transcriptional downregulation of the bile acid importer Na+-taurocholate co-transporting protein (NTCP) and to ER-stress in the liver. Here, we show that ER-stress induction strongly reduces NTCP protein expression, plasma membrane abundance and NTCP-mediat...
ORGANISM(S): Homo sapiens (Human) 
2019-01-07 | PXD007948 | Pride
Calnexin/ cholestasis/er-stress/ ntcp/calreticulin/xbp1/perk/lectin chaperones 
UnknownCalnexin deficiency leads to dysmyelination.
Not available
S-EPMC2881815 | biostudies-literature
UnknownEnhanced clathrin-dependent endocytosis in the absence of calnexin.
Not available
S-EPMC3128601 | biostudies-literature
UnknownModelling interaction between HIV-1 Nef and calnexin.
Not available
S-EPMC6136951 | biostudies-literature
UnknownCalnexin, More Than Just a Molecular Chaperone.
Not available
S-EPMC9913998 | biostudies-literature
UnknownArc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin.
Not available
S-EPMC5611444 | biostudies-literature
UnknownIntramembrane client recognition potentiates the chaperone functions of calnexin.
Not available
S-EPMC9753464 | biostudies-literature
UnknownCalnexin cycle - structural features of the ER chaperone system.
Not available
S-EPMC7687155 | biostudies-literature
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