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Calumin, a novel Ca2+-binding transmembrane protein on the
endoplasmic reticulum.
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 57928
Author(s) Zhang, Miao; Yamazaki, Tetsuo; Yazawa, Masayuki; Treves, Susan; Nishi, Miyuki; Murai, Machiko;
Shibata, Eisuke; Zorzato, Francesco; Takeshima, Hiroshi
Author(s) at UniBasel Treves, Susan;
Year 2007
Title Calumin, a novel Ca2+-binding transmembrane protein on the endoplasmic reticulum.
Journal Cell Calcium
Volume 42
Number 1
Pages / Article-Number 83-90
We have identified a novel endoplasmic reticulum (ER)-resident protein, named "calumin", which is expressed
in various tissues. This protein has a molecular mass of approximately 60 kDa and is composed of an ERluminal domain rich in acidic residues, a single transmembrane segment, and a large cytoplasmic domain.
Biochemical experiments demonstrated that the amino-terminal luminal domain is capable of binding Ca2+
with a high capacity and moderate affinity. In embryonic fibroblasts derived from calumin-knockout mice
exhibiting embryonic and neonatal lethality, fluorometric Ca2+ imaging detected insufficient Ca2+ contents in
intracellular stores and attenuated store-operated Ca2+ entry. Moreover, the mutant fibroblasts were highly
sensitive to cell death induced by ER stress. These observations suggest that calumin plays an essential role
in ER Ca2+ handling and is also implicated in signaling from the ER, which is closely associated with cell-fate
decision.
Publisher Elsevier
ISSN/ISBN 0143-4160
edoc-URL http://edoc.unibas.ch/45311/
Full Text on edoc
Restricted
Digital Object Identifier DOI 10.1016/j.ceca.2006.11.009
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/17204322
ISI-Number WOS:000247296700008
Document type (ISI) Journal Article
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