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• W173823944 abstract "Research Article1 November 1992free access The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins. G. Simos G. Simos Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. Search for more papers by this author S.D. Georgatos S.D. Georgatos Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. Search for more papers by this author G. Simos G. Simos Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. Search for more papers by this author S.D. Georgatos S.D. Georgatos Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. Search for more papers by this author Author Information G. Simos1 and S.D. Georgatos1 1Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. The EMBO Journal (1992)11:4027-4036https://doi.org/10.1002/j.1460-2075.1992.tb05496.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info p58, also referred to as the lamin B receptor, is an intrinsic protein of the inner nuclear membrane that binds in vitro to lamin B. Previous studies have demonstrated that p58 is phosphorylated in vivo and removal of its phosphate moieties affects lamin B binding. Using affinity-purified antipeptide antibodies, we have now immunoisolated p58 from bird erythrocyte lysates under isotonic, non-denaturing conditions. Analysis of the immunopurified material shows that five distinct proteins are tightly and specifically associated with p58. Two of these polypeptides can be identified as nuclear lamins A and B. The immunoisolate also contains a kinase activity that phosphorylates p58 in vivo and in vitro, exclusively at serine residues, as indicated by phosphoamino acid analysis and two-dimensional phosphopeptide mapping. Cell fractionation experiments and in vitro phosphorylation assays demonstrate that the p58 kinase resides in the nuclear envelope and is distinct from protein kinase A and cdc2 kinase, for both of which p58 is an in vitro substrate. These data suggest that p58 is interacting in vivo with a p58 kinase and the nuclear lamins. Previous ArticleNext Article Volume 11Issue 111 November 1992In this issue RelatedDetailsLoading ..." @default.
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• W173823944 title "The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins." @default.
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• W173823944 doi "https://doi.org/10.1002/j.1460-2075.1992.tb05496.x" @default.
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