کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767907 | 1050801 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Caenorhabditis elegans calnexin is N-glycosylated and required for stress response
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 2, 16 December 2005, Pages 1018-1030
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 2, 16 December 2005, Pages 1018-1030
نویسندگان
Wonhae Lee, Tae Hoon Lee, Byung-Jae Park, Jong-Wook Chang, Jae-Ran Yu, Hyun-Sook Koo, Hyun Park, Yung Joon Yoo, Joohong Ahnn,