ArticleThe EMBO journal1992
The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 93 citations in OpenAlex.
- Antagonistic contributions of A-type and B-type lamins to LBR localization and dynamics.Nucleus (Austin, Tex.) · 2026Article
- Antagonistic contributions of A-type and B-type lamins to LBR localization and dynamics.bioRxiv : the preprint server for biology · 2026Article
- Comprehending a Killer: The Akt/mTOR Signaling Pathways Are Temporally High-Jacked by the Highly Pathogenic 1918 Influenza Virus.EBioMedicine · 2018Article
- Article
- Lamin B receptor regulates the growth and maturation of myeloid progenitors via its sterol reductase domain: implications for cholesterol biosynthesis in regulating myelopoiesis.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Requirement for lamin B receptor and its regulation by importin {beta} and phosphorylation in nuclear envelope assembly during mitotic exit.The Journal of biological chemistry · 2010Article
- The lamin B receptor under transcriptional control of C/EBPepsilon is required for morphological but not functional maturation of neutrophils.Human molecular genetics · 2008Article
- Granulocytic nuclear differentiation of lamin B receptor-deficient mouse EPRO cells.Experimental hematology · 2008Article
- The E1circumflexE4 protein of human papillomavirus interacts with the serine-arginine-specific protein kinase SRPK1.Journal of virology · 2007Article
- The genome and the nucleus: a marriage made by evolution. Genome organisation and nuclear architecture.Chromosoma · 2005Review
- Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection.Journal of virology · 2001Article
- The inner nuclear membrane: simple, or very complex?The EMBO journal · 2001Review
- MAF1, a novel plant protein interacting with matrix attachment region binding protein MFP1, is located at the nuclear envelope.The Plant cell · 1999Article
- Roles of LAP2 proteins in nuclear assembly and DNA replication: truncated LAP2beta proteins alter lamina assembly, envelope formation, nuclear size, and DNA replication efficiency in Xenopus laevis extracts.The Journal of cell biology · 1999Article
- An ordered inheritance strategy for the Golgi apparatus: visualization of mitotic disassembly reveals a role for the mitotic spindle.The Journal of cell biology · 1998Article
- Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis.The Journal of cell biology · 1997Article
- The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles.The EMBO journal · 1997Article
- The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope.The EMBO journal · 1996Article
- Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein.The Journal of cell biology · 1996Article
- Immunolocalization of lamins and nuclear pore complex proteins by atomic force microscopy.Pflugers Archiv : European journal of physiology · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.