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Blasig IE Winkler L Lassowski B Mueller SL Zuleger N Krause E Krause G Gast K Kolbe M Piontek J 《Cellular and molecular life sciences : CMLS》2006,63(4):505-514
Tight junctions seal intercellular clefts via membrane-related strands, hence, maintaining important organ functions. We investigated
the self-association of strand-forming transmembrane tight junction proteins. The regulatory tight junction protein occludin
was differently tagged and cotransfected in eucaryotic cells. These occludins colocalized within the plasma membrane of the
same cell, coprecipitated and exhibited fluorescence resonance energy transfer. Differently tagged strand-forming claudin-5
also colocalized in the plasma membrane of the same cell and showed fluorescence resonance energy transfer. This demonstrates
self-association in intact cells both of occludin and claudin-5 in one plasma membrane. In search of dimerizing regions of
occludin, dimerization of its cytosolic C-terminal coiledcoil domain was identified. In claudin-5, the second extracellular
loop was detected as a dimer. Since the transmembrane junctional adhesion molecule also is known to dimerize, the assumption
that homodimerization of transmembrane tight junction proteins may serve as a common structural feature in tight junction
assembly is supported.
Received 6 October 2005; received after revision 14 December 2005; accepted 27 December 2005
†These authors contributed equally to this work. 相似文献
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The inner nuclear membrane harbors a unique set of membrane proteins, many of which interact with nuclear intermediate filaments and chromatin components and thus play an important role in nuclear organization and gene expression regulation. These membrane proteins have to be constantly transported into the nucleus from their sites of synthesis in the ER to match the growth of the nuclear membrane during interphase. Many mechanisms have evolved to enable translocation of these proteins to the nucleus. The full range of mechanisms goes from rare autophagy events to regulated translocation using the nuclear pore complexes. Though mechanisms involving nuclear pores are predominant, within this group an enormous mechanistic range is observed from free diffusion through the peripheral channels to many distinct mechanisms involving different nucleoporins and other components of the soluble protein transport machinery in the central channels. This review aims to provide a comprehensive insight into this mechanistic diversity. 相似文献
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Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope 总被引:1,自引:1,他引:0
Poonam Malik Nadia Korfali Vlastimil Srsen Vassiliki Lazou Dzmitry G. Batrakou Nikolaj Zuleger Deirdre M. Kavanagh Gavin S. Wilkie Martin W. Goldberg Eric C. Schirmer 《Cellular and molecular life sciences : CMLS》2010,67(8):1353-1369
Nuclear envelope complexity is expanding with respect to identification of protein components. Here we test the validity of
proteomics results that identified 67 novel predicted nuclear envelope transmembrane proteins (NETs) from liver by directly
comparing 30 as tagged fusions using targeting assays. This confirmed 21 as NETs, but 4 only targeted in certain cell types,
underscoring the complexity of interactions that tether NETs to the nuclear envelope. Four NETs accumulated at the nuclear
rim in normal fibroblasts but not in fibroblasts lacking lamin A, suggesting involvement of lamin A in tethering them in the
nucleus. However, intriguingly, for the NETs tested alternative mechanisms for nuclear envelope retention could be found in
Jurkat cells that normally lack lamin A. This study expands by a factor of three the number of liver NETs analyzed, bringing
the total confirmed to 31, and shows that several have multiple mechanisms for nuclear envelope retention. 相似文献
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