Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum

被引：210

作者：

Gelebart, P

Opas, M

Michalak, M ^{[1
]}

机构：

[1] Univ Alberta, Canadian Inst Hlth Res Membrane Prot Res Grp, Edmonton, AB T6G 2H7, Canada

[2] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada

[3] Univ Toronto, Dept Pathol & Lab Med, Toronto, ON M5S 1A8, Canada

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2005年 / 37卷 / 02期

关键词：

endoplasmic reticulum; chaperone; protein folding; calcium homeostasis;

D O I：

10.1016/j.biocel.2004.02.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calreticulin is a 46-kDa Ca2+-binding chaperone found across a diverse range of species. The protein is involved in the regulation of intracellular Ca2+ homeostasis and endoplasmic reticulum (ER) Ca2+ storage capacity. Calreticulin is also an important molecular chaperone involved in "quality control" within secretory pathways. The protein contains structurally and functionally unique domains with specialized functions. Studies on calreticulin knockout mice indicate that the protein is essential in early cardiac development. The protein also plays an important role in autoimmunity and cancer. (C) 2004 Elsevier Ltd. All rights reserved.

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页码：260 / 266

页数：7

相关论文

共 26 条

[1] Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria [J].

Arnaudeau, S ;

Frieden, M ;

Nakamura, K ;

Castelbou, C ;

Michalak, M ;

Demaurex, N .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (48) :46696-46705

[2] Endoplasmic reticulum of animal cells and its organization into structural and functional domains [J].

Baumann, O ;

Walz, B .

INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL 205, 2001, 205 :149-214

[3] NMR structures of 36 and 73-residue fragments of the calreticulin P-domain [J].

Ellgaard, L ;

Bettendorff, P ;

Braun, D ;

Herrmann, T ;

Fiorito, F ;

Jelesarov, M ;

Güntert, P ;

Helenius, A ;

Wüthrich, K .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 322 (04) :773-784

[4] NMR structure of the calreticulin P-domain [J].

Ellgaard, L ;

Riek, R ;

Herrmann, T ;

Güntert, P ;

Braun, D ;

Helenius, A ;

Wüthrich, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (06) :3133-3138

[5] Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin [J].

Gao, B ;

Adhikari, R ;

Howarth, M ;

Nakamura, K ;

Gold, MC ;

Hill, AB ;

Knee, R ;

Michalak, M ;

Elliott, T .

IMMUNITY, 2002, 16 (01) :99-109

[6] Identification of an N-domain histidine essential for chaperone function in calreticulin [J].

Guo, L ;

Groenendyk, J ;

Papp, S ;

Dabrowska, M ;

Knoblach, B ;

Kay, C ;

Parker, JMR ;

Opas, M ;

Michalak, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (50) :50645-50653

[7] Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse [J].

Guo, L ;

Nakamura, K ;

Lynch, J ;

Opas, M ;

Olson, EN ;

Agellon, LB ;

Michalak, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (52) :50776-50779

[8] Apoptotic cell removal [J].

Henson, PM ;

Bratton, DL ;

Fadok, VA .

CURRENT BIOLOGY, 2001, 11 (19) :R795-R805

[9] The ins and outs of calreticulin: from the ER lumen to the extracellular space [J].

Johnson, S ;

Michalak, M ;

Opas, M ;

Eggleton, P .

TRENDS IN CELL BIOLOGY, 2001, 11 (03) :122-129

[10] Calreticulin is essential for cardiac development [J].

Mesaeli, N ;

Nakamura, K ;

Zvaritch, E ;

Dickie, P ;

Dziak, E ;

Krause, KH ;

Opas, M ;

MacLennan, DH ;

Michalak, M .

JOURNAL OF CELL BIOLOGY, 1999, 144 (05) :857-868