ArticleCells2016
Src1 is a Protein of the Inner Nuclear Membrane Interacting with the Dictyostelium Lamin NE81.
Article in Cells, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 23 citations in OpenAlex.
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- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.bioRxiv : the preprint server for biology · 2024Article
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- Heterologous expression ofMolecular biology of the cell · 2024Article
- Lamins as structural nuclear elements through evolution.Current opinion in cell biology · 2023Review
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- Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021Review
- Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast.Cells · 2020Review
- In Vivo Assembly of aCells · 2020Article
- Proteins of the Nucleolus ofCells · 2019Review
- Supramolecular Structures of theCells · 2019Article
- Identification of the evolutionarily conserved nuclear envelope proteins Lem2 and MicLem2 inGene: X · 2019Article
- Efficient proximity labeling in living cells and organisms with TurboID.Nature biotechnology · 2018Article
- Proximity-dependent labeling methods for proteomic profiling in living cells.Wiley interdisciplinary reviews. Developmental biology · 2017Review
- Filling the Void: Proximity-Based Labeling of Proteins in Living Cells.Trends in cell biology · 2016Review
- Meet the neighbors: Mapping local protein interactomes by proximity-dependent labeling with BioID.Proteomics · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear envelope (NE) consists of the outer and inner nuclear membrane (INM), whereby the latter is bound to the nuclear lamina. Src1 is a Dictyostelium homologue of the helix-extension-helix family of proteins, which also includes the human lamin-binding protein MAN1. Both endogenous Src1 and GFP-Src1 are localized to the NE during the entire cell cycle. Immuno-electron microscopy and light microscopy after differential detergent treatment indicated that Src1 resides in the INM. FRAP experiments with GFP-Src1 cells suggested that at least a fraction of the protein could be stably engaged in forming the nuclear lamina together with the Dictyostelium lamin NE81. Both a BioID proximity assay and mis-localization of soluble, truncated mRFP-Src1 at cytosolic clusters consisting of an intentionally mis-localized mutant of GFP-NE81 confirmed an interaction of Src1 and NE81. Expression GFP-Src1(1-646), a fragment C-terminally truncated after the first transmembrane domain, disrupted interaction of nuclear membranes with the nuclear lamina, as cells formed protrusions of the NE that were dependent on cytoskeletal pulling forces. Protrusions were dependent on intact microtubules but not actin filaments. Our results indicate that Src1 is required for integrity of the NE and highlight Dictyostelium as a promising model for the evolution of nuclear architecture.
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