title: Calreticulin, a calcium-binding molecular chaperone, is required for stress response and fertility in Caenorhabditis elegans.
abstract: Calreticulin (CRT), a Ca(2+)-binding protein known to have many cellular functions, including regulation of Ca(2+) homoeostasis and chaperone activity, is essential for heart and brain development during embryogenesis in mice. Here, we report the functional characterization of Caenorhabditis elegans calreticulin (crt-1). A crt-1 null mutant does not result in embryonic lethality but shows temperature-dependent reproduction defects. In C. elegans CRT-1 is expressed in the intestine, pharynx, body-wall muscles, head neurons, coelomocytes, and in sperm. crt-1 males exhibit reduced mating efficiency and defects late in sperm development in addition to defects in oocyte development and/or somatic gonad function in hermaphrodites. Furthermore, crt-1 and itr-1 (inositol triphosphate receptor) together are required for normal behavioral rhythms. crt-1 transcript level is elevated under stress conditions, suggesting that CRT-1 may be important for stress-induced chaperoning function in C. elegans.
authors.affiliation: Department of Life Science, Kwangju Institute of Science and Technology, Kwangju, 500-712, Korea.
authors.forename: B J
authors.initials: BJ
authors.lastname: Park
authors.forename: D G
authors.initials: DG
authors.lastname: Lee
authors.forename: J R
authors.initials: JR
authors.lastname: Yu
authors.forename: S K
authors.initials: SK
authors.lastname: Jung
authors.forename: K
authors.initials: K
authors.lastname: Choi
authors.forename: J
authors.initials: J
authors.lastname: Lee
authors.forename: J
authors.initials: J
authors.lastname: Lee
authors.forename: Y S
authors.initials: YS
authors.lastname: Kim
authors.forename: J I
authors.initials: JI
authors.lastname: Lee
authors.forename: J Y
authors.initials: JY
authors.lastname: Kwon
authors.forename: J
authors.initials: J
authors.lastname: Lee
authors.forename: A
authors.initials: A
authors.lastname: Singson
authors.forename: W K
authors.initials: WK
authors.lastname: Song
authors.forename: S H
authors.initials: SH
authors.lastname: Eom
authors.forename: C S
authors.initials: CS
authors.lastname: Park
authors.forename: D H
authors.initials: DH
authors.lastname: Kim
authors.forename: J
authors.initials: J
authors.lastname: Bandyopadhyay
authors.forename: J
authors.initials: J
authors.lastname: Ahnn
mesh_terms: D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D037282:Calreticulin; D005298:Fertility / Q000235:genetics; D017353:Gene Deletion; D020869:Gene Expression Profiling; D006706:Homeostasis; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D053496:Inositol 1,4,5-Trisphosphate Receptors; D007413:Intestinal Mucosa / Q000378:metabolism; D008297:Male; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism; D010614:Pharynx / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism; D012261:Ribonucleoproteins / Q000235:genetics / Q000378:metabolism*; D013094:Spermatozoa / Q000378:metabolism; D013696:Temperature
chemical_list: D029742:Caenorhabditis elegans Proteins; D015220:Calcium Channels; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D053496:Inositol 1,4,5-Trisphosphate Receptors; D018832:Molecular Chaperones; D012333:RNA, Messenger; D018160:Receptors, Cytoplasmic and Nuclear; D012261:Ribonucleoproteins; D002118:Calcium