Caenorhabditis elegans calnexin is N-glycosylated and required for stress response

Wonhae Lee, Tae Hoon Lee, Byung Jae Park, Jong Wook Chang, Jae Ran Yu, Hyun Sook Koo, Hyun Park, Yung Joon Yoo, Joohong Ahnn

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


Calnexin, a type I integral Ca2+-binding protein in the endoplasmic reticulum (ER) membrane, has been implicated in various biological functions including chaperone activity, calcium homeostasis, phagocytosis, and ER stress-induced apoptosis. Caenorhabditis elegans CNX-1 is expressed in the H-shaped excretory cell, intestine, dorsal and ventral nerve cord, spermatheca, and head and tail neurons throughout development. A cnx-1 null mutant displays temperature-sensitive developmental and reproductive defects, and retarded growth under stress. Moreover, a double knockout mutant of calnexin and calreticulin exhibits additive severe defects. Interestingly, both cnx-1 transcript and protein levels are elevated under stress conditions suggesting that CNX-1 may be important for stress-induced chaperoning functions in C. elegans. Glycosidase treatment and site-directed mutagenesis confirmed that CeCNX-1 is N-glycosylated at two asparagine residues of Asn203 and Asn571. When transgenic animals from cnx-1 mutant were generated, a glycosylation defective construct failed to rescue phenotypes of cnx-1 mutant suggesting that glycosylation is important for calnexin's functions in C. elegans.

Original languageEnglish
Pages (from-to)1018-1030
Number of pages13
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2005 Dec 16

Bibliographical note

Funding Information:
We thank A. Coulson for cosmids, the CGC for worm strains, A. Fire for expression vectors, and Y. Kohara for yk clones. We are especially grateful to C. Johnson for giving strains, L. Vanoaica for manuscript preparation, and M. Kim for computing 3D structure of CeCNX-1. This work was supported by the grant (M103KV010019-04K2201-01920) from the Korea Ministry of Science and Technology.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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