Calumin, a novel Ca2+-binding transmembrane protein on the endoplasmic reticulum.

Zhang, Miao and Yamazaki, Tetsuo and Yazawa, Masayuki and Treves, Susan and Nishi, Miyuki and Murai, Machiko and Shibata, Eisuke and Zorzato, Francesco and Takeshima, Hiroshi. (2007) Calumin, a novel Ca2+-binding transmembrane protein on the endoplasmic reticulum. Cell Calcium, 42 (1). pp. 83-90.

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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 ER-luminal 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.
Faculties and Departments:03 Faculty of Medicine > Departement Biomedizin > Department of Biomedicine, University Hospital Basel > Perioperative Patient Safety (Girard/Treves)
UniBasel Contributors:Treves, Susan
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:31 May 2017 09:30
Deposited On:20 Dec 2016 14:05

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