Lamin B constitutes an intermediate filament attachment site at the nuclear envelope.

@article{Georgatos1987LaminBC,
  title={Lamin B constitutes an intermediate filament attachment site at the nuclear envelope.},
  author={Spyros D. Georgatos and G{\"u}nter Blobel},
  journal={The Journal of cell biology},
  year={1987},
  volume={105 1},
  pages={117-25}
}
We found that urea extraction of turkey erythrocyte nuclear envelopes abolished their ability to bind exogenous 125I-vimentin, while, at the same time, it removed the nuclear lamins from the membranes. After purification of the lamins from such urea extracts, a specific binding between isolated vimentin and lamin B, or a lamin A + B hetero-oligomer, was detected by affinity chromatography. Similar analysis revealed that the 6.6-kD vimentin tail piece was involved in this interaction. By other… CONTINUE READING
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