ArticleMethods in enzymology2019
Methodologies to monitor protein turnover at the inner nuclear membrane.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.The Journal of cell biology · 2025Article
- Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins.Cell reports · 2022Article
- Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities.Nature cell biology · 2022Article
- p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells.International journal of molecular sciences · 2022Article
- Design and synthesis of a novel nanocomposite based on magnetic dopamine nanoparticles for purification of α-amylase from the bovine milk.Scientific reports · 2021Article
- Cell-type-specific, multicolor labeling of endogenous proteins with split fluorescent protein tags inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Lipid and protein dynamics that shape nuclear envelope identity.Molecular biology of the cell · 2020Review
- Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2.The Journal of cell biology · 2020Article
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lamin B receptor (LBR) is an inner nuclear membrane protein that associates with the nuclear lamina and harbors sterol reductase activity essential for cholesterol biosynthesis. Several LBR mutations implicated in human congenital disorders give rise to C-terminal truncations which render LBR metabolically unstable, resulting in their rapid turnover in the nucleus. These LBR variants serve as model substrates for investigating the poorly understood protein quality control pathways in the mammalian nuclear envelope (NE). Here we describe a split-GFP-based method for tagging these model substrates to enable live cell imaging and flow cytometry for the identification and characterization of NE-resident protein turnover machinery. Furthermore, we describe a facile subcellular fractionation method to isolate a soluble LBR degradation intermediate, allowing the deconvolution of the membrane extraction and proteasomal turnover steps. The combination of imaging-based and biochemical approaches described here facilitates detailed mechanistic studies to dissect protein turnover in the nuclear compartment.
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Registered trials
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