THE 1ST MEMBRANE SPANNING REGION OF THE LAMIN-B RECEPTOR IS SUFFICIENT FOR SORTING TO THE INNER NUCLEAR-MEMBRANE

被引:117
作者
SMITH, S
BLOBEL, G
机构
[1] Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York
关键词
D O I
10.1083/jcb.120.3.631
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The lamin B receptor (LBR) is a polytopic integral membrane protein localized exclusively in the inner nuclear membrane domain of the nuclear envelope. Its cDNA deduced primary structure consists of a highly charged amino-terminal domain of 205 residues that faces the nucleoplasm followed by a hydrophobic domain with eight potential transmembrane segments. To identify determinants that sort LBR from its site of integration (RER and outer nuclear membrane) to the inner nuclear membrane, we prepared full-length, truncated, and chimeric cDNA constructs of chick LBR, transfected these into mammalian cells and detected the expressed protein by immunofluorescence microscopy using appropriate antibodies. Surprisingly, we found that the determinants for sorting of LBR to the inner nuclear membrane reside in a region comprising its first transmembrane sequence plus flanking residues on either side. The other transmembrane regions as well as the nucleoplasmic domain are not required for sorting. We propose that the first transmembrane segment of LBR interacts specifically with another transmembrane segment and consider several mechanisms by which such specific interaction could result in sorting to the inner nuclear membrane.
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页码:631 / 637
页数:7
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