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. 1988 Nov;85(22):8531–8534. doi: 10.1073/pnas.85.22.8531

A lamin B receptor in the nuclear envelope.

H J Worman 1, J Yuan 1, G Blobel 1, S D Georgatos 1
PMCID: PMC282492  PMID: 2847165

Abstract

Using a solution binding assay, we show that purified 125I-labeled lamin B binds in a saturable and specific fashion to lamin-depleted avian erythrocyte nuclear membranes with a Kd of approximately 0.2 microM. This binding is significantly greater than the binding of 125I-labeled lamin A and is competitively inhibited by unlabeled ligand. We demonstrate that a 58-kDa integral membrane protein (p58) is a lamin B receptor by virtue of its abundance in the nuclear envelope and association with 125I-labeled lamin B in ligand blotting assays. Specific antibodies raised against p58 recognize one protein in isolated nuclei and partially block 125I-labeled lamin B binding to lamin-depleted nuclear membranes. Cell fractionation and indirect immunofluorescence microscopy show that p58 is located in the periphery of the nucleus. This protein may serve as a membrane attachment site for the nuclear lamina by acting as a specific receptor for lamin B.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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