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J. Biol. Chem., Vol. 277, Issue 8, 6422-6427, February 22, 2002
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From the Department of Physiology, Johns Hopkins University School
of Medicine, Baltimore, Maryland 21205
The discovery and biochemical characterization of
the secretory pathway Ca2+-ATPase, PMR1, in
Saccharomyces cerevisiae, has paved the way for
identification of PMR1 homologues in many species including rat,
Caenorhabditis elegans, and Homo sapiens. In
yeast, PMR1 has been shown to function as a high affinity
Ca2+/Mn2+ pump and has been localized to the
Golgi compartment where it is important for protein sorting,
processing, and glycosylation. However, little is known about PMR1
homologues in higher organisms. Loss of one functional allele of the
human gene, hSPCA1, has been linked to Hailey-Hailey disease,
characterized by skin ulceration and improper keratinocyte adhesion. We
demonstrate that expression of hSPCA1 in yeast fully complements
pmr1 phenotypes of hypersensitivity to Ca2+
chelators and Mn2+ toxicity. Similar to PMR1,
epitope-tagged hSPCA1 also resides in the Golgi when expressed in yeast
or in chinese hamster ovary cells. 45Ca2+
transport by hSPCA1 into isolated yeast Golgi vesicles shows an
apparent Ca2+ affinity of 0.26 µM, is
inhibitable by Mn2+, but is
thapsigargin-insensitive. In contrast, heterologous expression of vertebrate sarcoplasmic reticulum and plasma membrane
Ca2+-ATPases in yeast complement the Ca2+- but
not Mn2+-related phenotypes of the pmr1-null
strain, suggesting that high affinity Mn2+ transport is a
unique feature of the secretory pathway Ca2+-ATPases.
Functional Expression in Yeast of the Human Secretory Pathway
Ca2+, Mn2+-ATPase Defective in Hailey-Hailey
Disease*
,
*
This work was supported by Grant GM62142 from the National
Institutes of Health (to R. R.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Indian Inst. of Chemical Biology, 4, Raja S. C.
Mullick Road, Jadavpur, Calcutta, 700032 West Bengal, India.
§
To whom correspondence should be addressed. Tel.: 410-955-4732;
Fax: 410-955-0461; E-mail: rrao@jhmi.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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