ArticleThe Journal of cell biology1995
Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 216 citations in OpenAlex.
- Detection of nuclear STING in cultured human cells and in the normal and cancer tissues.iScience · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Sense, plug, and seal: proteins as both rapid responders and constitutive barriers supporting organelle compartmentalization.Molecular biology of the cell · 2025Review
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- Deciphering Spatial Protein-Protein Interactions in Brain Using Proximity Labeling.Molecular & cellular proteomics : MCP · 2022Review
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Molecular Pathology of Laminopathies.Annual review of pathology · 2022Review
- Article
- The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021Review
- Nuclear lipid droplets form in the inner nuclear membrane in a seipin-independent manner.The Journal of cell biology · 2021Article
- Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores.Nature communications · 2020Article
- Lamin is essential for nuclear localization of the GPI synthesis enzyme PIG-B and GPI-anchored protein production inJournal of cell science · 2020Article
- Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane.The Journal of biological chemistry · 2019Article
- Pathogenic mutations in genes encoding nuclear envelope proteins and defective nucleocytoplasmic connections.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Casting a Wider Net: Differentiating between Inner Nuclear Envelope and Outer Nuclear Envelope Transmembrane Proteins.International journal of molecular sciences · 2019Review
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- Review
- Article
- Systematic analysis of NLMP suggests nuclear localization of RTK/MET kinases resemble cancer cell clearance.Journal of experimental & clinical cancer research : CR · 2019Article
- Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane.International journal of molecular sciences · 2019Article
25 more citing papers are in PubMed but not listed here.
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
We have examined transfected cells by immunofluorescence microscopy to determine the signals and structural features required for the targeting of integral membrane proteins to the inner nuclear membrane. Lamin B receptor (LBR) is a resident protein of the nuclear envelope inner membrane that has a nucleoplasmic, amino-terminal domain and a carboxyl-terminal domain with eight putative transmembrane segments. The amino-terminal domain of LBR can target both a cytosolic protein to the nucleus and a type II integral protein to the inner nuclear membrane. Neither a nuclear localization signal (NLS) of a soluble protein, nor full-length histone H1, can target an integral protein to the inner nuclear membrane although they can target cytosolic proteins to the nucleus. The addition of an NLS to a protein normally located in the inner nuclear membrane, however, does not inhibit its targeting. When the amino-terminal domain of LBR is increased in size from approximately 22.5 to approximately 70 kD, the chimeric protein cannot reach the inner nuclear membrane. The carboxyl-terminal domain of LBR, separated from the amino-terminal domain, also concentrates in the inner nuclear membrane, demonstrating two nonoverlapping targeting signals in this protein. Signals and structural features required for the inner nuclear membrane targeting of proteins are distinct from those involved in targeting soluble polypeptides to the nucleoplasm. The structure of the nucleocytoplasmic domain of an inner nuclear membrane protein also influences targeting, possibly because of size constraints dictated by the lateral channels of the nuclear pore complexes.
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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.