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J. Biol. Chem., Vol. 276, Issue 18, 15330-15336, May 4, 2001
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From the Mammalian selenocysteine-containing
proteins characterized with respect to function are involved in redox
processes and exhibit distinct expression patterns and cellular
locations. A recently identified 15-kDa selenoprotein (Sep15) has no
homology to previously characterized proteins, and its function is not
known. Here we report the intracellular localization and identification
of a binding partner for this selenoprotein which implicate Sep15 in the regulation of protein folding. The native Sep15 isolated from rat
prostate and mouse liver occurred in a complex with a 150-kDa protein.
The latter protein was identified as UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which was previously shown to be involved in the quality control of protein folding. UGTR functions by glucosylating misfolded proteins, retaining them in the ER until they are correctly folded or
transferring them to degradation pathways. To determine the intracellular localization of Sep15, we expressed a green fluorescent protein-Sep15 fusion protein in CV-1 cells, and this protein was localized to the ER and possibly other perinuclear compartments. We
determined that Sep15 contained the N-terminal signal peptide that was
essential for translocation and that it was cleaved in the mature
protein. However, C-terminal sequences of Sep15 were not involved in
trafficking and retention of Sep15. The data suggest that the
association between Sep15 and UGTR is responsible for maintaining the
selenoprotein in the ER. This report provides the first example of the
ER-resident selenoprotein and suggests a possible role of the trace
element selenium in the quality control of protein folding.
Association between the 15-kDa Selenoprotein and
UDP-glucose:Glycoprotein Glucosyltransferase in the Endoplasmic
Reticulum of Mammalian Cells*
,
Department of Biochemistry and the
¶ Center for Biotechnology, University of Nebraska, Lincoln,
Nebraska 68588-0664 and the § Basic Research Laboratory,
NCI, National Institutes of Health, Bethesda, Maryland 20892
*
This work was supported by grants from Cancer Research
Foundation of America and the National Institutes of Health (to
V. N. G.).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.
To whom correspondence should be addressed: Dept. of
Biochemistry, University of Nebraska, N151 Beadle Center, Lincoln, NE 68588-0664. Fax: 402-472-7842; E-mail: vgladyshev1@unl.edu.
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