ArticleMethods in enzymology2016
BioID Identification of Lamin-Associated Proteins.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Attenuated lamin A-prohibitin2 interaction leads to mitochondrial dysfunction in LMNA 289 A>G-mediated dilated cardiomyopathy.The Journal of biological chemistry · 2026Article
- Defining the interactome of the pancreas-specific SPCA2 isoform (SPCA2C) identifies unique links to store-operated CaThe FEBS journal · 2025Article
- Leveraging a self-cleaving peptide for tailored control in proximity labeling proteomics.Cell reports methods · 2024Article
- Liver-derived plasminogen mediates muscle stem cell expansion during caloric restriction through the plasminogen receptor Plg-RCell reports · 2024Article
- The development of proximity labeling technology and its applications in mammals, plants, and microorganisms.Cell communication and signaling : CCS · 2023Review
- Article
- Nuclear Compartments: An Incomplete Primer to Nuclear Compartments, Bodies, and Genome Organization Relative to Nuclear Architecture.Cold Spring Harbor perspectives in biology · 2022Review
- Parvovirus nonstructural protein 2 interacts with chromatin-regulating cellular proteins.PLoS pathogens · 2022Article
- The Nuclear Lamina.Cold Spring Harbor perspectives in biology · 2022Review
- A method to map the interaction network of the nuclear lamina with genetically encoded photo-crosslinkersFrontiers in chemistry · 2022Article
- Proximity-dependent biotinylation detects associations between SARS coronavirus nonstructural protein 1 and stress granule-associated proteins.The Journal of biological chemistry · 2021Article
- Mapping Proximity Associations of Core Spindle Assembly Checkpoint Proteins.Journal of proteome research · 2021Article
- Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.Life science alliance · 2021Article
- Proximal Protein Interaction Landscape of RAS Paralogs.Cancers · 2020Article
- The MyMOMA domain of MYO19 encodes for distinct Miro-dependent and Miro-independent mechanisms of interaction with mitochondrial membranes.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Towards improving proximity labeling by the biotin ligase BirA.Methods (San Diego, Calif.) · 2019Article
- A proximity-tagging system to identify membrane protein-protein interactions.Nature methods · 2018Article
- The proximity-labeling technique BioID identifies sorting nexin 6 as a member of the insulin-like growth factor 1 (IGF1)-IGF1 receptor pathway.The Journal of biological chemistry · 2018Article
- Review
- An improved smaller biotin ligase for BioID proximity labeling.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
A- and B-type lamins support the nuclear envelope, contribute to heterochromatin organization, and regulate a myriad of nuclear processes. The mechanisms by which lamins function in different cell types and the mechanisms by which lamin mutations cause over a dozen human diseases (laminopathies) remain unclear. The identification of proteins associated with lamins is likely to provide fundamental insight into these mechanisms. BioID (proximity-dependent biotin identification) is a unique and powerful method for identifying protein-protein and proximity-based interactions in living cells. BioID utilizes a mutant biotin ligase from bacteria that is fused to a protein of interest (bait). When expressed in living cells and stimulated with excess biotin, this BioID-fusion protein promiscuously biotinylates directly interacting and vicinal endogenous proteins. Following biotin-affinity capture, the biotinylated proteins can be identified using mass spectrometry. BioID thus enables screening for physiologically relevant protein associations that occur over time in living cells. BioID is applicable to insoluble proteins such as lamins that are often refractory to study by other methods and can identify weak and/or transient interactions. We discuss the use of BioID to elucidate novel lamin-interacting proteins and its applications in a broad range of biological systems, and provide detailed protocols to guide new applications.
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Registered trials
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.