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

Full Abstract

Calnexin, a type I integral Ca(2+)-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 Asn(203) and Asn(571). 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.

Author information

Author/s: Lee, Wonhae (W); Lee, Tae Hoon (TH); Park, Byung-Jae (BJ); Chang, Jong-Wook (JW); Yu, Jae-Ran (JR); Koo, Hyun-Sook (HS); Park, Hyun (H); Yoo, Yung Joon (YJ); Ahnn, Joohong (J);

Affiliation: Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun), published in United States. (Language: eng)

Reference: 2005-Dec; vol 338 (issue 2) : pp 1018-30

Dates: Created 2005/11/15; Completed 2006/01/12; Revised 2006/11/15;

PMID: 16256074, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

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