CANX binds Glu1Man9GlcNAc2-CDH1

Stable Identifier
R-HSA-9932988
Type
Reaction [uncertain]
Species
Homo sapiens
Compartment
ReviewStatus
3/5
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After Glucosidase II complex-mediated removal of the second glucose residue, the Glu1Man9GlcNAc2-proteoglycans enter the so-called calnexin/calreticulin cycle, binding to chaperones CANX (calnexin) (membrane-bound glycoproteins) or CALR (calreticulin) (soluble glycoproteins), which ensure proper folding of nascent glycoproteins (reviewed in Helenius and Aebi 2004). CDH1 binds to CANX, and the binding is increased for recombinant mutant CDH1 proteins that are unable to be properly glycosylated and are, thus, likely misfolded (Zhou et al. 2008). CALR positively affects presentation of CDH1 on the plasma membrane, with CALR knockdown leading to decreased plasma membrane levels of CDH1 and accumulation of CDH1 in cis Golgi (Iwahashi et al. 2019). No binding between CDH1 and calreticulin has been tested (Iwahashi et al. 2019) and the effect of CALR on CDH1 plasma membrane presentation may be indirect.
Literature References
PubMed ID Title Journal Year
18491227 Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD

Zhou, F, Su, J, Fu, L, Yang, Y, Zhang, L, Wang, L, Zhao, H, Zhang, D, Li, Z, Zha, X

Glycoconj J 2008
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