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Journal articles on the topic 'TurboID'

Author: Grafiati

Published: 9 November 2024

Last updated: 31 July 2025

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1

Cho, Kelvin F., Tess C. Branon, Sanjana Rajeev, et al. "Split-TurboID enables contact-dependent proximity labeling in cells." Proceedings of the National Academy of Sciences 117, no. 22 (2020): 12143–54. http://dx.doi.org/10.1073/pnas.1919528117.

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Proximity labeling catalyzed by promiscuous enzymes, such as TurboID, have enabled the proteomic analysis of subcellular regions difficult or impossible to access by conventional fractionation-based approaches. Yet some cellular regions, such as organelle contact sites, remain out of reach for current PL methods. To address this limitation, we split the enzyme TurboID into two inactive fragments that recombine when driven together by a protein–protein interaction or membrane–membrane apposition. At endoplasmic reticulum–mitochondria contact sites, reconstituted TurboID catalyzed spatially rest

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2

Cho, Kelvin F., Tess C. Branon, Namrata D. Udeshi, Samuel A. Myers, Steven A. Carr, and Alice Y. Ting. "Proximity labeling in mammalian cells with TurboID and split-TurboID." Nature Protocols 15, no. 12 (2020): 3971–99. http://dx.doi.org/10.1038/s41596-020-0399-0.

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3

May, Danielle G., Kelsey L. Scott, Alexandre R. Campos, and Kyle J. Roux. "Comparative Application of BioID and TurboID for Protein-Proximity Biotinylation." Cells 9, no. 5 (2020): 1070. http://dx.doi.org/10.3390/cells9051070.

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BioID is a well-established method for identifying protein–protein interactions and has been utilized within live cells and several animal models. However, the conventional labeling period requires 15–18 h for robust biotinylation which may not be ideal for some applications. Recently, two new ligases termed TurboID and miniTurbo were developed using directed evolution of the BioID ligase and were able to produce robust biotinylation following a 10 min incubation with excess biotin. However, there is reported concern about inducibility of biotinylation, cellular toxicity, and ligase stability.

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4

Doerr, Allison. "Proximity labeling with TurboID." Nature Methods 15, no. 10 (2018): 764. http://dx.doi.org/10.1038/s41592-018-0158-0.

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Garloff, Vera, and Ignacio Rubio. "Schneller, weiter, TurboID – Modulation einer übereifrigen Biotin-Ligase." BIOspektrum 29, no. 3 (2023): 273–75. http://dx.doi.org/10.1007/s12268-023-1943-6.

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AbstractProtein-protein interactions are key elements of intracellular signalling and metabolic pathways. These interactions can be revealed with the help of proximity ligation screens, prominently biotinylation screens. This approach has profited from the recent development of the highly active biotin ligase TurboID, which however also led to problems of toxicity related to its high basal activity. We have established a simple protocol to improve TurboID performance and enhance protein functionality.

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Makhsatova, S. A., A. B. Kurmanbay, I. A. Akhmetollayev, and A. T. Kulyyassov. "ASSEMBLING THE TURBOID-CONTAINING PLASMID CONSTRUCT FOR INVESTIGATING THE IN VIVO PROTEIN-PROTEIN INTERACTIONS." Eurasian Journal of Applied Biotechnology, no. 3S (September 12, 2024): 47. http://dx.doi.org/10.11134/btp.3s.2024.35.

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In vivo interactions between biomolecules (Proteins, RNA, and DNA) are the basis of cellular functionality including cell cycle, signaling pathways, cellular metabolism, and other biological processes. The traditional methods for detecting protein-protein interactions, such as affinity purification and two-hybrid analysis have limitations for the in-depth study of the cellular proteome. Besides, proteomics of the organelle protein components is still challenging to study, due to the spatial and temporal dynamics of proteins. To address these problems, proximity labeling technology was introduc

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Takano, Tetsuya. "Comprehensive identification of molecules at synapses and non-synaptic cell-adhesion structure." Impact 2023, no. 3 (2023): 46–48. http://dx.doi.org/10.21820/23987073.2023.3.46.

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The brain is incredibly complex and there is so much we don't know about this organ and its mechanisms. Assistant Professor Tetsuya Takano, School of Medicine, Keio University, Japan, is working to better understand neuroscience. One area of interest is neurons and astrocytes; specifically elucidating the protein component functions in each neural circuit. He and his team are working to shed light on the pathological mechanism of psychiatric and neurological disorders and, in doing so, enabling improved treatments and benefiting patients across the globe. The team has developed spatio-temporal

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8

Russo, Marissa, Emily Norton-Ramos, Maria Jose Ulloa Navas, Alfredo Quinones-Hinojosa, and Hugo Guerrero-Cazares. "Abstract 6579: Elucidating glioblastoma-derived extracellular vesicle cargo using TurboID: Implications for tumor microenvironment adaptation." Cancer Research 85, no. 8_Supplement_1 (2025): 6579. https://doi.org/10.1158/1538-7445.am2025-6579.

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Abstract Glioblastoma (GBM), the most aggressive primary brain tumor in adults, presents significant challenges due to its universal recurrence and limited survival rates, exacerbated when proximal to the lateral ventricles (LV). The subpopulation of brain tumor-initiating cells (BTICs) plays a pivotal role in tumor initiation and invasiveness, interacting with the microenvironment, particularly the cellular components in the subventricular zone (SVZ). Some mechanisms of intercellular communication present in the SVZ include paracrine, autocrine, direct cell contact, gap junctions, nanotubes,

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9

Rabinovich-Ernst, Orna, Clinton Bradfield, SungHwan Yoon, et al. "TurboID biotin-tagging mass spectrometry identifies specific caspase-11-associated proteins regulating non-canonical inflammasome activation." Journal of Immunology 206, no. 1_Supplement (2021): 15.06. http://dx.doi.org/10.4049/jimmunol.206.supp.15.06.

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Abstract While it has been demonstrated that cytosolic LPS can directly activate caspase11, the cellular processes regulating the non-canonical inflammasome response remain poorly defined. Caspase11 and caspase1 show substantial structural similarity, however, unlike the activation of caspase1 by NLR inflammasomes, there are no sensor or adaptor proteins known to be involved in transmitting cytosolic LPS signal to caspase11. Also, while caspase11 has been shown to associate with LPS, it lacks a characteristic LPS binding domain as observed in many other LPS binding proteins such as MD2 and LBP

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10

Kim, Han Byeol, and Kwang-eun Kim. "Precision proteomics with TurboID: mapping the suborganelle landscape." Korean Journal of Physiology & Pharmacology 28, no. 6 (2024): 495–501. http://dx.doi.org/10.4196/kjpp.2024.28.6.495.

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11

Qian, Lijuan, Yuxin He, Wenzhe Lian, et al. "AgrC biotinylation inhibits Staphylococcus aureus infection." PLOS ONE 20, no. 4 (2025): e0318695. https://doi.org/10.1371/journal.pone.0318695.

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Staphylococcus aureus (S. aureus) is a leading cause of nosocomial infections, particularly among antibiotic-resistant strains. S. aureus virulence is governed by the accessory gene regulator (Agr) quorum sensing (QS) system, which relies on AgrC, a two-component histidine kinase, to detect secreted auto-inducing peptides (AIPs). Emerging evidence highlights the potential of inhibiting the interaction between AgrC and AIPs as a promising therapeutic strategy. Given the limited clinic methods in inhibiting AgrC, we hereby report a novel method utilizing TurboID, an engineered biotin ligase, to

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12

Gurung, Sadeechya. "Abstract 998: Extracellular proximity labeling (ePL) as a tool to identify protein-protein interactions in the tumor microenvironment." Cancer Research 82, no. 12_Supplement (2022): 998. http://dx.doi.org/10.1158/1538-7445.am2022-998.

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Abstract The extracellular matrix (ECM) is a dynamic niche that is extensively reshaped in the development of the tumor microenvironment (TME). Our current understanding of ECM function and dynamics is largely informed by identification of protein-protein interactions (PPIs) using co-immunoprecipitation (co-IP) techniques that may miss transient and weak/unstable interactions. Recent advances in proximity labeling techniques have greatly expanded the interactome networks of numerous intracellular proteins, however these tools have yet to be extended to study PPIs in the ECM. We have recently o

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13

Teplova, Anastasia D., Marina V. Serebryakova, Raisa A. Galiullina, Nina V. Chichkova, and Andrey B. Vartapetian. "Identification of Phytaspase Interactors via the Proximity-Dependent Biotin-Based Identification Approach." International Journal of Molecular Sciences 22, no. 23 (2021): 13123. http://dx.doi.org/10.3390/ijms222313123.

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Proteolytic enzymes are instrumental in various aspects of plant development, including senescence. This may be due not only to their digestive activity, which enables protein utilization, but also to fulfilling regulatory functions. Indeed, for the largest family of plant serine proteases, subtilisin-like proteases (subtilases), several members of which have been implicated in leaf and plant senescence, both non-specific proteolysis and regulatory protein processing have been documented. Here, we strived to identify the protein partners of phytaspase, a plant subtilase involved in stress-indu

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14

Gomes-Junior, Rubens, Claudia Maria do Nascimento Moreira, and Bruno Dallagiovanna. "Construction of a proximity labeling vector to identify protein-protein interactions in human stem cells." PLOS One 20, no. 5 (2025): e0324779. https://doi.org/10.1371/journal.pone.0324779.

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Identification of protein-protein interactions is essential for understanding protein functions in biological processes. While immunoprecipitation has traditionally been used to isolate proteins and their partners, it faces limitations in capturing transient interactions. Proximity labeling, particularly with the biotin ligase TurboID, addresses this challenge by enabling rapid and efficient identification of interacting proteins in vivo. Human induced pluripotent stem cells are valuable models for studying human development, however certain biological processes, such as differentiation, can b

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15

Branon, Tess C., Justin A. Bosch, Ariana D. Sanchez, et al. "Efficient proximity labeling in living cells and organisms with TurboID." Nature Biotechnology 36, no. 9 (2018): 880–87. http://dx.doi.org/10.1038/nbt.4201.

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16

Holzer, Elisabeth, Cornelia Rumpf-Kienzl, Sebastian Falk, and Alexander Dammermann. "A modified TurboID approach identifies tissue-specific centriolar components in C. elegans." PLOS Genetics 18, no. 4 (2022): e1010150. http://dx.doi.org/10.1371/journal.pgen.1010150.

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Proximity-dependent labeling approaches such as BioID have been a great boon to studies of protein-protein interactions in the context of cytoskeletal structures such as centrosomes which are poorly amenable to traditional biochemical approaches like immunoprecipitation and tandem affinity purification. Yet, these methods have so far not been applied extensively to invertebrate experimental models such as C. elegans given the long labeling times required for the original promiscuous biotin ligase variant BirA*. Here, we show that the recently developed variant TurboID successfully probes the i

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17

Peeney, David, Sadeechya Gurung, Josh Rich, Sasha Coates-Park, Yueqin Liu, and William G. Stetler-Stevenson. "Abstract 2348: Mapping the interactome of matrisome targets using extracellular proximity labeling (ePL)." Cancer Research 83, no. 7_Supplement (2023): 2348. http://dx.doi.org/10.1158/1538-7445.am2023-2348.

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Abstract Classical methods to investigate protein-protein interactions (PPIs) are generally performed in non-living systems, yet in recent years new technologies utilizing proximity labeling (PL) have given researchers the tools to explore PPIs in living systems. PL has distinct advantages over traditional protein interactome studies, such as the ability to identify weak and transient interactions in vitro and in vivo. Most PL studies are performed on targets within or on the cell membrane. We describe a method to investigate PPIs within the extracellular compartment, using both BioID2 and Tur

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18

Artan, Murat, Stephen Barratt, Sean M. Flynn, et al. "Interactome analysis of Caenorhabditis elegans synapses by TurboID-based proximity labeling." Journal of Biological Chemistry 297, no. 3 (2021): 101094. http://dx.doi.org/10.1016/j.jbc.2021.101094.

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19

Smirnova, Evgeniya V., Tatiana V. Rakitina, Rustam H. Ziganshin, et al. "Identification of Myelin Basic Protein Proximity Interactome Using TurboID Labeling Proteomics." Cells 12, no. 6 (2023): 944. http://dx.doi.org/10.3390/cells12060944.

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Myelin basic protein (MBP) is one of the key structural elements of the myelin sheath and has autoantigenic properties in multiple sclerosis (MS). Its intracellular interaction network is still partially deconvoluted due to the unfolded structure, abnormally basic charge, and specific cellular localization. Here we used the fusion protein of MBP with TurboID, an engineered biotin ligase that uses ATP to convert biotin to reactive biotin-AMP that covalently attaches to nearby proteins, to determine MBP interactome. Despite evident benefits, the proximity labeling proteomics technique generates

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20

Fujimoto, Shintaro, Shinya Tashiro, and Yasushi Tamura. "Complementation Assay Using Fusion of Split-GFP and TurboID (CsFiND) Enables Simultaneous Visualization and Proximity Labeling of Organelle Contact Sites in Yeast." Contact 6 (January 2023): 251525642311536. http://dx.doi.org/10.1177/25152564231153621.

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Numerous studies have revealed that organelle membrane contact sites (MCSs) play important roles in diverse cellular events, including the transport of lipids and ions between connected organelles. To understand MCS functions, it is essential to uncover proteins that accumulate at MCSs. Here, we develop a complementation assay system termed CsFiND (Complementation assay using Fusion of split-GFP and TurboID) for the simultaneous visualization of MCSs and identification of MCS-localized proteins. We express the CsFiND proteins on the endoplasmic reticulum and mitochondrial outer membrane in yea

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21

Artan, Murat, Stephen Barratt, Sean M. Flynn, et al. "Correction: Interactome analysis of Caenorhabditis elegans synapses by TurboID-based proximity labeling." Journal of Biological Chemistry 298, no. 6 (2022): 102081. http://dx.doi.org/10.1016/j.jbc.2022.102081.

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22

Branon, Tess C., Justin A. Bosch, Ariana D. Sanchez, et al. "Author Correction: Efficient proximity labeling in living cells and organisms with TurboID." Nature Biotechnology 38, no. 1 (2019): 108. http://dx.doi.org/10.1038/s41587-019-0355-0.

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23

Wang, Chenyu, and Laidong Yu. "TurboID Proximity Labeling of a Protocadherin Protein to Characterize Interacting Protein Complex." American Journal of Molecular Biology 13, no. 04 (2023): 213–26. http://dx.doi.org/10.4236/ajmb.2023.134015.

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24

Wei, Xia-fei, Shan Li, and Jie-li Hu. "A TurboID-based proximity labelling approach for identifying the DNA-binding proteins." STAR Protocols 4, no. 1 (2023): 102139. http://dx.doi.org/10.1016/j.xpro.2023.102139.

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25

Schaan Profes, Marcos, Araven Tiroumalechetty, Neel Patel, Stephanie S. Lauar, Simone Sidoli, and Peri T. Kurshan. "Characterization of the intracellular neurexin interactome by in vivo proximity ligation suggests its involvement in presynaptic actin assembly." PLOS Biology 22, no. 1 (2024): e3002466. http://dx.doi.org/10.1371/journal.pbio.3002466.

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Neurexins are highly spliced transmembrane cell adhesion molecules that bind an array of partners via their extracellular domains. However, much less is known about the signaling pathways downstream of neurexin’s largely invariant intracellular domain (ICD). Caenorhabditis elegans contains a single neurexin gene that we have previously shown is required for presynaptic assembly and stabilization. To gain insight into the signaling pathways mediating neurexin’s presynaptic functions, we employed a proximity ligation method, endogenously tagging neurexin’s intracellular domain with the promiscuo

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de Groot, Adriaan F., Zowi R. Huinen, Juan Simon Nieto, and Daniel S. Peeper. "Abstract 3960: Genome-wide CRISPR screens for genes inhibiting T cell-tumor cell interactions identify complex N-glycans." Cancer Research 85, no. 8_Supplement_1 (2025): 3960. https://doi.org/10.1158/1538-7445.am2025-3960.

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The efficacy of immunotherapy fundamentally depends on effective T cell-tumor cell interactions, yet the molecular determinants orchestrating this engagement are not fully understood. Here, we systematically mapped and perturbed key regulators of the T cell-tumor cell interactome using innovative cell-cell interaction assays. We performed genome-wide CRISPR screens to identify genes critically required for physical and functional interactions between T cells and tumor cells. Using TurboID proximity labeling and T cell-tumor cell conjugates, we identified the complex N-glycan biosynthesis pathw

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Kanzler, Charlotte R., Michael Donohue, Megan E. Dowdle, and Michael D. Sheets. "TurboID functions as an efficient biotin ligase for BioID applications in Xenopus embryos." Developmental Biology 492 (December 2022): 133–38. http://dx.doi.org/10.1016/j.ydbio.2022.10.005.

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Holzer, Elisabeth, Cornelia Rumpf-Kienzl, Sebastian Falk, and Alexander Dammermann. "Correction: A modified TurboID approach identifies tissue-specific centriolar components in C. elegans." PLOS Genetics 19, no. 2 (2023): e1010645. http://dx.doi.org/10.1371/journal.pgen.1010645.

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Santana, Maria Sissa Pereira, Vivian Petersen Wagner, Felipe Paiva Fonseca, Colin D. Bingle, and Lynne Bingle. "Adenoid cystic carcinoma interactome: exploring MYB and MYB-NFIB protein interactions with turboid." Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology 139, no. 5 (2025): e106. https://doi.org/10.1016/j.oooo.2025.01.531.

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30

Larochelle, Marc, Danny Bergeron, Bruno Arcand, and François Bachand. "Proximity-dependent biotinylation mediated by TurboID to identify protein–protein interaction networks in yeast." Journal of Cell Science 132, no. 11 (2019): jcs232249. http://dx.doi.org/10.1242/jcs.232249.

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31

Gottschalk, Robert, Leah Wachsmuth, Dingyin Tao, et al. "Abstract 2657: SNAP-TurboID: A Proximity-based Intracellular Tool for Small Molecule Target Identification." Journal of Biological Chemistry 299, no. 3 (2023): S156. http://dx.doi.org/10.1016/j.jbc.2023.103345.

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32

Petersen, Max, Kiayla Washington, Anna Dorota Chorzalska, and Patrycja M. Dubielecka. "Proximity Proteomics Identifies a Role of MAP2K4 (MKK4) in JAK2 V617F Signaling." Blood 144, Supplement 1 (2024): 2721. https://doi.org/10.1182/blood-2024-212028.

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JAK inhibitors reduce symptomatic burden of myeloproliferative neoplasms (MPN), including attenuation of disease-driving JAK-STAT activation, but their curative efficacy is limited. To identify non-canonical activities of JAK that contribute to disease pathology, we used proximity dependent biotin labeling followed by mass spectrometry of JAK2 V617F and JAK2 enabled by enhanced biotin ligase TurboID. Using proximity labeling-based proteomics, supported by our newly developed proximity proteomics data bioinformatics analysis pipeline, we performed a systematic analysis of spatially restricted J

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Li, Haorong, Ashley M. Frankenfield, Ryan Houston, Shiori Sekine, and Ling Hao. "Thiol-Cleavable Biotin for Chemical and Enzymatic Biotinylation and Its Application to Mitochondrial TurboID Proteomics." Journal of the American Society for Mass Spectrometry 32, no. 9 (2021): 2358–65. http://dx.doi.org/10.1021/jasms.1c00079.

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34

Yan, Biao, Ting Zeng, Xiaoshan Liu, et al. "Study on the interaction protein of transcription factor Smad3 based on TurboID proximity labeling technology." Genomics 116, no. 3 (2024): 110839. http://dx.doi.org/10.1016/j.ygeno.2024.110839.

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35

Hu, Yaofang, Changsheng Jiang, Yueqiao Zhao, et al. "TurboID screening of ApxI toxin interactants identifies host proteins involved in Actinobacillus pleuropneumoniae-induced apoptosis of immortalized porcine alveolar macrophages." Veterinary Research 54, no. 1 (2023). http://dx.doi.org/10.1186/s13567-023-01194-6.

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AbstractActinobacillus pleuropneumoniae (APP) is a gram-negative pathogenic bacterium responsible for porcine contagious pleuropneumonia (PCP), which can cause porcine necrotizing and hemorrhagic pleuropneumonia. Actinobacillus pleuropneumoniae-RTX-toxin (Apx) is an APP virulence factor. APP secretes a total of four Apx toxins, among which, ApxI demonstrates strong hemolytic activity and cytotoxicity, causing lysis of porcine erythrocytes and apoptosis of porcine alveolar macrophages. However, the protein interaction network between this toxin and host cells is still poorly understood. TurboID

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Wang, Bo, Fan Yang, Wuqian Wang, Fei Zhao, and Xiaofang Sun. "TurboID-mediated proximity labeling technologies to identify virus co-receptors." Frontiers in Cellular and Infection Microbiology 14 (June 27, 2024). http://dx.doi.org/10.3389/fcimb.2024.1371837.

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Virus receptors determine the tissue tropism of viruses and have a certain relationship with the clinical outcomes caused by viral infection, which is of great importance for the identification of virus receptors to understand the infection mechanism of viruses and to develop entry inhibitor. Proximity labeling (PL) is a new technique for studying protein-protein interactions, but it has not yet been applied to the identification of virus receptors or co-receptors. Here, we attempt to identify co-receptor of SARS-CoV-2 by employing TurboID-catalyzed PL. The membrane protein angiotensin-convert

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Mair, Andrea, Shou-Ling Xu, Tess C. Branon, Alice Y. Ting, and Dominique C. Bergmann. "Proximity labeling of protein complexes and cell-type-specific organellar proteomes in Arabidopsis enabled by TurboID." eLife 8 (September 19, 2019). http://dx.doi.org/10.7554/elife.47864.

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Defining specific protein interactions and spatially or temporally restricted local proteomes improves our understanding of all cellular processes, but obtaining such data is challenging, especially for rare proteins, cell types, or events. Proximity labeling enables discovery of protein neighborhoods defining functional complexes and/or organellar protein compositions. Recent technological improvements, namely two highly active biotin ligase variants (TurboID and miniTurbo), allowed us to address two challenging questions in plants: (1) what are in vivo partners of a low abundant key developm

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Shafraz, Omer, Carolyn Marie Orduno Davis, and Sanjeevi Sivasankar. "Light Activated BioID (LAB): an optically activated proximity labeling system to study protein-protein interactions." Journal of Cell Science, September 27, 2023. http://dx.doi.org/10.1242/jcs.261430.

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Proximity labeling with genetically encoded enzymes are widely used to study protein-protein interactions in cells. However, the accuracy of proximity labeling is limited by a lack of control over the enzymatic labeling process. Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision. Our technology, called Light Activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1. We demonstrate in multiple cell lines, that up

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Kushner, Jared S., Aaron Rodriques, Sergey Zakharov, Alexander Katchman, STAVROS FANOURAKIS, and Steven Marx. "Abstract 12045: Mapping the CaV1.2 Interactome in Rat Heart in vivo." Circulation 146, Suppl_1 (2022). http://dx.doi.org/10.1161/circ.146.suppl_1.12045.

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Introduction: The Ca2+ channel CaV1.2 is an essential part of excitation contraction coupling, neurotransmission and vascular tone. Identifying protein partners of CaV1.2 is critical to make mechanistic insights into these fundamental processes. Prior CaV1.2 proximity proteomes used APEX labeling, which labels other amino acids, introduces oxidative stress and is catalyzed ex vivo. Hypothesis: α1C-TurboID knockin rats can generate tissue specific interactomes in vivo, in cells with intact cell and matrix contacts, which may differ substantially from interactomes made from ex vivo peroxidase ca

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Zhang, Bo, Yuanbing Zhang, and Ji-Long Liu. "Highly effective proximate labeling in Drosophila." G3 Genes|Genomes|Genetics 11, no. 5 (2021). http://dx.doi.org/10.1093/g3journal/jkab077.

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Abstract The protein–protein interaction (PPI) is a basic strategy for life to operate. The analysis of PPIs in multicellular organisms is very important but extremely challenging because PPIs are particularly dynamic and variable among different development stages, tissues, cells, and even organelles. Therefore, understanding PPI needs a good resolution of time and space. More importantly, understanding in vivo PPI needs to be realized in situ. Proximity-based biotinylation combined with mass spectrometry (MS) has emerged as a powerful approach to study PPI networks and protein subcellular co

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Su, Yanting, Yuanyuan Guo, Jieyu Guo, Ting Zeng, Ting Wang, and Wu Liu. "Study of FOXO1-interacting proteins using TurboID-based proximity labeling technology." BMC Genomics 24, no. 1 (2023). http://dx.doi.org/10.1186/s12864-023-09238-z.

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Abstract Background Protein‒protein interactions (PPIs) are the foundation of the life activities of cells. TurboID is a biotin ligase with higher catalytic efficiency than BioID or APEX that reduces the required labeling time from 18 h to 10 min. Since many proteins participate in binding and catalytic events that are very short-lived, it is theoretically possible to find relatively novel binding proteins using the TurboID technique. Cell proliferation, apoptosis, autophagy, oxidative stress and metabolic disorders underlie many diseases, and forkhead box transcription factor 1 (FOXO1) plays

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Szczesniak, Laura M., Caden G. Bonzerato, and Richard J. H. Wojcikiewicz. "Identification of the Bok Interactome Using Proximity Labeling." Frontiers in Cell and Developmental Biology 9 (May 31, 2021). http://dx.doi.org/10.3389/fcell.2021.689951.

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The function of the Bcl-2 family member Bok is currently enigmatic, with various disparate roles reported, including mediation of apoptosis, regulation of mitochondrial morphology, binding to inositol 1,4,5-trisphosphate receptors, and regulation of uridine metabolism. To better define the roles of Bok, we examined its interactome using TurboID-mediated proximity labeling in HeLa cells, in which Bok knock-out leads to mitochondrial fragmentation and Bok overexpression leads to apoptosis. Labeling with TurboID-Bok revealed that Bok was proximal to a wide array of proteins, particularly those in

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Lau, Chun Sing, Adam Dowle, Gavin H. Thomas, Philipp Girr, and Luke C. M. Mackinder. "A phase-separated CO2-fixing pyrenoid proteome determined by TurboID in Chlamydomonas reinhardtii." Plant Cell, May 17, 2023. http://dx.doi.org/10.1093/plcell/koad131.

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Abstract Phase separation underpins many biologically important cellular events such as RNA metabolism, signaling and CO2 fixation. However, determining the composition of a phase-separated organelle is often challenging due to its sensitivity to environmental conditions, which limits the application of traditional proteomics techniques like organellar purification or affinity purification mass spectrometry to understand their composition. In Chlamydomonas reinhardtii, Rubisco is condensed into a crucial phase-separated organelle called the pyrenoid that improves photosynthetic performance by

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Li, Xiaofang, Yanping Wei, Qili Fei, Guilin Fu, Yu Gan, and Chuanlin Shi. "TurboID‐mediated proximity labeling for screening interacting proteins of FIP37 in Arabidopsis." Plant Direct 7, no. 12 (2023). http://dx.doi.org/10.1002/pld3.555.

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AbstractProximity labeling was recently developed to detect protein–protein interactions and members of subcellular multiprotein structures in living cells. Proximity labeling is conducted by fusing an engineered enzyme with catalytic activity, such as biotin ligase, to a protein of interest (bait protein) to biotinylate adjacent proteins. The biotinylated protein can be purified by streptavidin beads, and identified by mass spectrometry (MS). TurboID is an engineered biotin ligase with high catalytic efficiency, which is used for proximity labeling. Although TurboID‐based proximity labeling t

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Yheskel, Matanel, Simone Sidoli, and Julie Secombe. "Proximity labeling reveals a new in vivo network of interactors for the histone demethylase KDM5." Epigenetics & Chromatin 16, no. 1 (2023). http://dx.doi.org/10.1186/s13072-023-00481-y.

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Abstract Background KDM5 family proteins are multi-domain regulators of transcription that when dysregulated contribute to cancer and intellectual disability. KDM5 proteins can regulate transcription through their histone demethylase activity in addition to demethylase-independent gene regulatory functions that remain less characterized. To expand our understanding of the mechanisms that contribute to KDM5-mediated transcription regulation, we used TurboID proximity labeling to identify KDM5-interacting proteins. Results Using Drosophila melanogaster, we enriched for biotinylated proteins from

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Haidar-Ahmad, Nathaline, Kyle Tomaro, Mathieu Lavallée-Adam, and François-Xavier Campbell-Valois. "The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC in Shigella flexneri." mSphere, October 31, 2024. http://dx.doi.org/10.1128/msphere.00553-24.

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ABSTRACT Promiscuous biotin ligases derived from the bacterial enzyme BirA are used to identify proteins vicinal to a bait protein, thereby defining its proxisome. Despite the popularity of this approach, surprisingly little is known about its use in prokaryotes. Here, we compared the activity of four widely used promiscuous biotin ligases in the cytoplasm of Shigella flexneri , a pathogenic subgroup of Escherichia coli . Our data indicate that the kinetics of TurboID’s biotinylating activity is the highest of those tested. In addition, TurboID showed reduced interaction with the natural BirA

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Zhang, Kaixin, Yinyin Li, Tengbo Huang, and Ziwei Li. "Potential application of TurboID-based proximity labeling in studying the protein interaction network in plant response to abiotic stress." Frontiers in Plant Science 13 (August 16, 2022). http://dx.doi.org/10.3389/fpls.2022.974598.

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Abiotic stresses are major environmental conditions that reduce plant growth, productivity and quality. Protein-protein interaction (PPI) approaches can be used to screen stress-responsive proteins and reveal the mechanisms of protein response to various abiotic stresses. Biotin-based proximity labeling (PL) is a recently developed technique to label proximal proteins of a target protein. TurboID, a biotin ligase produced by directed evolution, has the advantages of non-toxicity, time-saving and high catalytic efficiency compared to other classic protein-labeling enzymes. TurboID-based PL has

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Zhang, Qianshen, Zhiyan Wen, Xin Zhang, et al. "RETICULON-LIKE PROTEIN B2 is a pro-viral factor co-opted for the biogenesis of viral replication organelles in plants." Plant Cell, May 22, 2023. http://dx.doi.org/10.1093/plcell/koad146.

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Abstract Endomembrane remodeling to form a viral replication complex (VRC) is crucial for a virus to establish infection in a host. Although the composition and function of VRCs have been intensively studied, host factors involved in the assembly of VRCs for plant RNA viruses have not been fully explored. TurboID-based proximity labeling (PL) has emerged as a robust tool for probing molecular interactions in planta. However, few studies have employed the TurboID-based PL technique for investigating plant virus replication. Here, we used Beet black scorch virus (BBSV), an endoplasmic reticulum

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Park, Sohyeon, Xiaorong Wang, Yajin Mo, et al. "Proximity Labeling Expansion Microscopy (PL-ExM) Evaluates Interactome Labeling Techniques." Journal of Materials Chemistry B, 2024. http://dx.doi.org/10.1039/d4tb00516c.

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Understanding protein-protein interactions (PPIs) through proximity labeling has revolutionized our comprehension of cellular mechanisms and pathology. Various proximity labeling techniques, such as HRP, APEX, BioID, TurboID, and µMap, have been...

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Chen, Rui, Ningxia Zhang, Yubin Zhou, and Ji Jing. "Optical Sensors and Actuators for Probing Proximity-Dependent Biotinylation in Living Cells." Frontiers in Cellular Neuroscience 16 (February 16, 2022). http://dx.doi.org/10.3389/fncel.2022.801644.

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Proximity-dependent biotinylation techniques have been gaining wide applications in the systematic analysis of protein-protein interactions (PPIs) on a proteome-wide scale in living cells. The engineered biotin ligase TurboID is among the most widely adopted given its enhanced biotinylation efficiency, but it faces the background biotinylation complication that might confound proteomic data interpretation. To address this issue, we report herein a set of split TurboID variants that can be reversibly assembled by using light (designated “OptoID”), which enable optogenetic control of biotinylati

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