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J. Cell Biol.,
Volume 142, Number 4, August 24, 1998 963-973
* Department of Biomedical Engineering, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908; In Xenopus laevis oocytes, overexpression of
calreticulin suppresses inositol 1,4,5-trisphosphate-induced Ca2+ oscillations in a manner consistent with
inhibition of Ca2+ uptake into the endoplasmic reticulum. Here we report that the alternatively spliced isoforms of the sarcoendoplasmic reticulum Ca2+-ATPase
(SERCA)2 gene display differential Ca2+ wave properties and sensitivity to modulation by calreticulin. We
demonstrate by glucosidase inhibition and site-directed
mutagenesis that a putative glycosylated residue
(N1036) in SERCA2b is critical in determining both the
selective targeting of calreticulin to SERCA2b and isoform functional differences. Calreticulin belongs to a
novel class of lectin ER chaperones that modulate immature protein folding. In addition to this role, we suggest that these chaperones dynamically modulate the
conformation of mature glycoproteins, thereby affecting their function.
Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San
Antonio, Texas 78245; and § Department of Physiology, University of Texas Health Science Center at San Antonio, San Antonio,
Texas 78284
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