Nuclear Lamins a and B1

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Nuclear Lamins a and B1

At the end of mitosis, the nuclear lamins assemble to form the nuclear lamina during nuclear envelope formation in daughter cells. We have fused A- and B-type nuclear lamins to the green fluorescent protein to study this process in living cells. The results reveal that the A- and B-type lamins exhibit different pathways of assembly. In the early stages of mitosis, both lamins are distributed th...

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Nuclear Lamins A and B1: Different Pathways of Assembly during Nuclear Envelope Formation in Living Cells

At the end of mitosis, the nuclear lamins assemble to form the nuclear lamina during nuclear envelope formation in daughter cells. We have fused Aand B-type nuclear lamins to the green fluorescent protein to study this process in living cells. The results reveal that the Aand B-type lamins exhibit different pathways of assembly. In the early stages of mitosis, both lamins are distributed throug...

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Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy

The nuclear lamina is a key structural element of the metazoan nucleus. However, the structural organization of the major proteins composing the lamina is poorly defined. Using three-dimensional structured illumination microscopy and computational image analysis, we characterized the supramolecular structures of lamin A, C, B1, and B2 in mouse embryo fibroblast nuclei. Each isoform forms a dist...

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Nuclear lamins in cancer.

Dysmorphic nuclei are commonly seen in cancers and provide strong motivation for studying the main structural proteins of nuclei, the lamins, in cancer. Past studies have also demonstrated the significance of microenvironment mechanics to cancer progression, which is extremely interesting because the lamina was recently shown to be mechanosensitive. Here, we review current knowledge relating ca...

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A role for nuclear lamins in nuclear envelope assembly

The molecular interactions responsible for nuclear envelope assembly after mitosis are not well understood. In this study, we demonstrate that a peptide consisting of the COOH-terminal domain of Xenopus lamin B3 (LB3T) prevents nuclear envelope assembly in Xenopus interphase extracts. Specifically, LB3T inhibits chromatin decondensation and blocks the formation of both the nuclear lamina-pore c...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2000

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.151.6.1155