Journal
TRENDS IN CELL BIOLOGY
Volume 11, Issue 3, Pages 122-129Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0962-8924(01)01926-2
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Calreticulin was first isolated 26 years ago. Since its discovery as a minor Ca(2+)binding protein of the sarcoplasmic reticulum, the appreciation of its importance has grown, and it is now recognized to be a multifunctional protein, most abundant in the endoplasmic reticulum (ER). The protein has well-recognized physiological roles in the ER as a molecular chaperone and Ca2+-signalling molecule. However, it has also been found in other membrane-bound organelles, at the cell surface and in the extracellular environment, where it has recently been shown to exert a number of physiological and pathological effects. Here, we will focus on these less-well-characterized functions of calreticulin.
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