The DOI matches its Crossref record.
A guided tour into subcellular colocalization analysis in light microscopy
Abstract
Summary: It is generally accepted that the functional compartmentalization of eukaryotic cells is reflected by the differential occurrence of proteins in their compartments. The location and physiological function of a protein are closely related; local information of a protein is thus crucial to understanding its role in biological processes. The visualization of proteins residing on intracellular structures by fluorescence microscopy has become a routine approach in cell biology and is increasingly used to assess their colocalization with well‐characterized markers. However, image‐analysis methods for colocalization studies are a field of contention and enigma. We have therefore undertaken to review the most currently used colocalization analysis methods, introducing the basic optical concepts important for image acquisition and subsequent analysis. We provide a summary of practical tips for image acquisition and treatment that should precede proper colocalization analysis. Furthermore, we discuss the application and feasibility of colocalization tools for various biological colocalization situations and discuss their respective strengths and weaknesses. We have created a novel toolbox for subcellular colocalization analysis under ImageJ, named JACoP, that integrates current global statistic methods and a novel object‐based approach.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Items 101–165 of 165
Mardones, G. A., Burgos, P. V., Brooks, D. A., Parkinson-Lawrence, E., Mattera, R., & Bonifacino, J. S. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-02-0190 · Cited by 52
Vevea, J. D., Kusick, G. F., Courtney, K. C., Chen, E., Watanabe, S., & Chapman, E. R. (2021) · eLife · doi:10.7554/elife.67261 · Cited by 51
Heat Shock Factor 2 Protects against Proteotoxicity by Maintaining Cell-Cell Adhesion
Joutsen, J., Da Silva, A. J., Luoto, J. C., Budzynski, M. A., Nylund, A. S., de Thonel, A., Concordet, J.-P., Mezger, V., Sabéran-Djoneidi, D., Henriksson, E., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.037 · Cited by 51
Cytoplasmic localization of sterol transcription factors Upc2p and Ecm22p in S. cerevisiae
Marie, C., Leyde, S., & White, T. C. (2008) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.07.004 · Cited by 47
Patton, M. S., Lodge, D. J., Morilak, D. A., & Girotti, M. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2016.236 · Cited by 44
Biogenesis of a bacterial metabolosome for propanediol utilization
Yang, M., Wenner, N., Dykes, G. F., Li, Y., Zhu, X., Sun, Y., Huang, F., Hinton, J. C. D., & Liu, L.-N. (2022) · Nature Communications · doi:10.1038/s41467-022-30608-w · Cited by 45
Baranger, K., Bonnet, A. E., Girard, S. D., Paumier, J.-M., García-González, L., Elmanaa, W., Bernard, A., Charrat, E., Stephan, D., Bauer, C., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00163 · Cited by 44
Hassiotis, S., Manavis, J., Blumbergs, P. C., Hattersley, K. J., Carosi, J. M., Kamei, M., & Sargeant, T. J. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.13913 · Cited by 44
Novel method to analyze post-yield mechanical properties at trabecular bone tissue level
Carretta, R., Luisier, B., Bernoulli, D., Stüssi, E., Müller, R., & Lorenzetti, S. (2013) · Journal of the Mechanical Behavior of Biomedical Materials · doi:10.1016/j.jmbbm.2012.12.003 · Cited by 43
Kovács, R. Á., Vadászi, H., Bulyáki, É., Török, G., Tóth, V., Mátyás, D., Kun, J., Hunyadi-Gulyás, É., Fedor, F. Z., Csincsi, Á., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.599771 · Cited by 43
Cavieres, V. A., González, A., Muñoz, V. C., Yefi, C. P., Bustamante, H. A., Barraza, R. R., Tapia-Rojas, C., Otth, C., Barrera, M. J., González, C., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0136313 · Cited by 43
Cell surface dynamics and cellular distribution of endogenous FcRn
D’Hooghe, L., Chalmers, A. D., Heywood, S., & Whitley, P. (2017) · PLOS ONE · doi:10.1371/journal.pone.0182695 · Cited by 42
Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation
Jansen, R. M., Peruzzo, R., Fromm, S. A., Yokom, A. L., Zoncu, R., & Hurley, J. H. (2022) · Science Advances · doi:10.1126/sciadv.add2926 · Cited by 42
Burette, A. C., Strehler, E. E., & Weinberg, R. J. (2009) · Journal of Comparative Neurology · doi:10.1002/cne.21909 · Cited by 40
The Rho-specific GAP protein DLC3 coordinates endocytic membrane trafficking
Braun, A. C., Hendrick, J., Eisler, S. A., Schmid, S., Hausser, A., & Olayioye, M. A. (2015) · Journal of Cell Science · doi:10.1242/jcs.163857 · Cited by 41
Capel, R. A., Bose, S. J., Collins, T. P., Rajasundaram, S., Ayagama, T., Zaccolo, M., Burton, R.-A. B., & Terrar, D. A. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00380.2020 · Cited by 40
Paumier, J.-M., Py, N. A., García-González, L., Bernard, A., Stephan, D., Louis, L., Checler, F., Khrestchatisky, M., Baranger, K., & Rivera, S. (2019) · The FASEB Journal · doi:10.1096/fj.201801076r · Cited by 40
A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle
Jansen, K. I., Iwanski, M. K., Burute, M., & Kapitein, L. C. (2023) · Journal of Cell Biology · doi:10.1083/jcb.202106105 · Cited by 39
Geier, E. G., Bourdenx, M., Storm, N. J., Cochran, J. N., Sirkis, D. W., Hwang, J.-H., Bonham, L. W., Ramos, E. M., Diaz, A., Van Berlo, V., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1925-9 · Cited by 39
Rovelet-Lecrux, A., Feuillette, S., Miguel, L., Schramm, C., Pernet, S., Quenez, O., Ségalas-Milazzo, I., Guilhaudis, L., Rousseau, S., Riou, G., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01294-4 · Cited by 38
Byrnes, A. E., Dominguez, S. L., Yen, C.-W., Laufer, B. I., Foreman, O., Reichelt, M., Lin, H., Sagolla, M., Hötzel, K., Ngu, H., et al. (2023) · Molecular Therapy - Nucleic Acids · doi:10.1016/j.omtn.2023.05.005 · Cited by 38
The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex
Fokin, A. I., David, V., Oguievetskaia, K., Derivery, E., Stone, C. E., Cao, L., Rocques, N., Molinie, N., Henriot, V., Aumont-Nicaise, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abd5956 · Cited by 37
Conrad, R., Stölting, G., Hendriks, J., Ruello, G., Kortzak, D., Jordan, N., Gensch, T., & Hidalgo, P. (2018) · iScience · doi:10.1016/j.isci.2018.08.012 · Cited by 35
Refining in vitro models for nanomaterial exposure to cells and tissues
Guggenheim, E. J., Milani, S., Röttgermann, P. J. F., Dusinska, M., Saout, C., Salvati, A., Rädler, J. O., & Lynch, I. (2018) · NanoImpact · doi:10.1016/j.impact.2018.02.008 · Cited by 36
A functional endosomal pathway is necessary for lysosome biogenesis in Drosophila
Jacomin, A.-C., Fauvarque, M.-O., & Taillebourg, E. (2016) · BMC Cell Biology · doi:10.1186/s12860-016-0115-7 · Cited by 36
Regulation of integrin trafficking, cell adhesion, and cell migration by WASH and the Arp2/3 complex
Duleh, S. N., & Welch, M. D. (2012) · Cytoskeleton · doi:10.1002/cm.21069 · Cited by 36
Emechebe, U., Kumar P, P., Rozenberg, J. M., Moore, B., Firment, A., Mirshahi, T., & Moon, A. M. (2016) · eLife · doi:10.7554/elife.07897 · Cited by 36
Muthukumar, G., Stevens, T. A., Inglis, A. J., Esantsi, T. K., Saunders, R. A., Schulte, F., Voorhees, R. M., Guna, A., & Weissman, J. S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.028 · Cited by 34
The polarity protein Scribble positions DLC3 at adherens junctions to regulate Rho signaling
Hendrick, J., Franz-Wachtel, M., Moeller, Y., Schmid, S., Macek, B., & Olayioye, M. A. (2016) · Journal of Cell Science · doi:10.1242/jcs.190074 · Cited by 32
Synthetic Par polarity induces cytoskeleton asymmetry in unpolarized mammalian cells
Watson, J. L., Krüger, L. K., Ben-Sasson, A. J., Bittleston, A., Shahbazi, M. N., Planelles-Herrero, V. J., Chambers, J. E., Manton, J. D., Baker, D., & Derivery, E. (2023) · Cell · doi:10.1016/j.cell.2023.08.034 · Cited by 32
Male-specific epistasis between WWC1 and TLN2 genes is associated with Alzheimer's disease
Gusareva, E. S., Twizere, J.-C., Sleegers, K., Dourlen, P., Abisambra, J. F., Meier, S., Cloyd, R., Weiss, B., Dermaut, B., Bessonov, K., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.08.001 · Cited by 32
The anti-viral dynamin family member MxB participates in mitochondrial integrity
Cao, H., Krueger, E. W., Chen, J., Drizyte-Miller, K., Schulz, M. E., & McNiven, M. A. (2020) · Nature Communications · doi:10.1038/s41467-020-14727-w · Cited by 25
Singh, T., Kang, D. H., Kim, T. W., Kong, H. J., Ryu, J. S., Jeon, S., Ahn, T. S., Jeong, D., Baek, M. J., & Im, J. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120904 · Cited by 26
Golgi-resident TRIO regulates membrane trafficking during neurite outgrowth
Tao, T., Sun, J., Peng, Y., Li, Y., Wang, P., Chen, X., Zhao, W., Zheng, Y.-Y., Wei, L., Wang, W., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007318 · Cited by 26
Ilie, A., Boucher, A., Park, J., Berghuis, A. M., McKinney, R. A., & Orlowski, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012614 · Cited by 24
Das, M., Mao, W., Shao, E., Tamhankar, S., Yu, G.-Q., Yu, X., Ho, K., Wang, X., Wang, J., & Mucke, L. (2021) · iScience · doi:10.1016/j.isci.2021.103245 · Cited by 21
DIP2 is a unique regulator of diacylglycerol lipid homeostasis in eukaryotes
Mondal, S., Kinatukara, P., Singh, S., Shambhavi, S., Patil, G. S., Dubey, N., Singh, S. H., Pal, B., Shekar, P. C., Kamat, S. S., et al. (2022) · eLife · doi:10.7554/elife.77665 · Cited by 19
Šimunić, I., Jagečić, D., Isaković, J., Dobrivojević Radmilović, M., & Mitrečić, D. (2024) · Scientific Reports · doi:10.1038/s41598-024-57650-6 · Cited by 18
García‐González, L., Paumier, J., Louis, L., Pilat, D., Bernard, A., Stephan, D., Jullien, N., Checler, F., Nivet, E., Khrestchatisky, M., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100593r · Cited by 16
NRF3 activates mTORC1 arginine-dependently for cancer cell viability
Hirose, S., Waku, T., Tani, M., Masuda, H., Endo, K., Ashitani, S., Aketa, I., Kitano, H., Nakada, S., Wada, A., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106045 · Cited by 15
Disrupting the transmembrane domain interface between PMP22 and MPZ causes peripheral neuropathy
(2024) · doi:10.1016/j.isci.2024.110989 · Cited by 15
The RNA binding proteins LARP4A and LARP4B promote sarcoma and carcinoma growth and metastasis
Coleman, J. C., Tattersall, L., Yianni, V., Knight, L., Yu, H., Hallett, S. R., Johnson, P., Caetano, A. J., Cosstick, C., Ridley, A. J., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109288 · Cited by 15
Sectoral activation of glia in an inducible mouse model of autosomal dominant retinitis pigmentosa
Massengill, M. T., Ash, N. F., Young, B. M., Ildefonso, C. J., & Lewin, A. S. (2020) · Scientific Reports · doi:10.1038/s41598-020-73749-y · Cited by 13
Li, X., Goult, B. T., Ballestrem, C., & Zacharchenko, T. (2023) · Open Biology · doi:10.1098/rsob.230058 · Cited by 13
Bhattacharjee, R., Hall, A. R., Mangione, M. C., Igarashi, M. G., Roberts-Galbraith, R. H., Chen, J.-S., Vavylonis, D., & Gould, K. L. (2023) · eLife · doi:10.7554/elife.83062 · Cited by 12
(2025) · doi:10.1091/mbc.e24-10-0486 · Cited by 11
TLNRD1 is a CCM complex component and regulates endothelial barrier integrity
Ball, N. J., Ghimire, S., Follain, G., Pajari, A. O., Wurzinger, D., Vaitkevičiūtė, M., Cowell, A. R., Berki, B., Ivaska, J., Paatero, I., et al. (2024) · Journal of Cell Biology · doi:10.1083/jcb.202310030 · Cited by 11
PICALM regulates cathepsin D processing and lysosomal function
Hattersley, K. J., Carosi, J. M., Hein, L. K., Bensalem, J., & Sargeant, T. J. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.07.024 · Cited by 10
Andersen, R. C., Schmidt, J. H., Rombach, J., Lycas, M. D., Christensen, N. R., Lund, V. K., Stapleton, D. S., Pedersen, S. S., Olsen, M. A., Stoklund, M., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci144904 · Cited by 10
Yeung, S. H., Lee, R. H., Cheng, G. W., Ma, I. W., Kofler, J., Kent, C., Ma, F., Herrup, K., Fornage, M., Arai, K., et al. (2024) · The FASEB Journal · doi:10.1096/fj.202400689rr · Cited by 10
Sekar, T. V., Elghonaimy, E. A., Swancutt, K. L., Diegeler, S., Gonzalez, I., Hamilton, C., Leung, P. Q., Meiler, J., Martina, C. E., Whitney, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43038-z · Cited by 8
A planar polarized MYO6-DOCK7-RAC1 axis promotes tissue fluidification in mammary epithelia
(2023) · doi:10.1016/j.celrep.2023.113001 · Cited by 8
Franklin, N. E., Bonham, C. A., Xhabija, B., & Vacratsis, P. O. (2013) · Journal of Cell Science · doi:10.1242/jcs.113928 · Cited by 8
Ashraf, R., Polasek-Sedlackova, H., Marini, V., Prochazkova, J., Hasanova, Z., Zacpalova, M., Boudova, M., & Krejci, L. (2025) · Nature Communications · doi:10.1038/s41467-025-56518-1 · Cited by 6
Pöhl, S., Osorio-Valeriano, M., Cserti, E., Harberding, J., Hernandez-Tamayo, R., Biboy, J., Sobetzko, P., Vollmer, W., Graumann, P. L., & Thanbichler, M. (2024) · eLife · doi:10.7554/elife.86577 · Cited by 5
Moretto, E., Masato, A., Panzi, C., Lopes, A. T., Stuart, S., De La-Rocque, S., Caso, M. G., White, I. J., Harris, S. S., Busche, M. A., et al. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02266-4 · Cited by 4
On the role of VP3-PI3P interaction in birnavirus endosomal membrane targeting
Zanetti, F. A., Fernandez, I., Baquero, E., Guardado-Calvo, P., Ferrino-Iriarte, A., Dubois, S., Morel, E., Alfonso, V., Aguilera, M. O., Celayes, M. E., et al. (2025) · eLife · doi:10.7554/elife.97261 · Cited by 4
Uncharacterized protein C17orf80 – a novel interactor of human mitochondrial nucleoids
(2023) · doi:10.1242/jcs.260822 · Cited by 3
Rapid ex vivo reverse genetics identifies the essential determinants of prion protein toxicity
Reimann, R. R., Puzio, M., Rosati, A., Emmenegger, M., Schneider, B. L., Valdés, P., Huang, D., Caflisch, A., & Aguzzi, A. (2023) · Brain Pathology · doi:10.1111/bpa.13130 · Cited by 3
On the Role of VP3-PI3P Interaction in Birnavirus Endosomal Membrane Targeting
(2024) · doi:10.1101/2024.02.20.581221 · Cited by 1
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
(2025) · doi:10.7554/elife.106839 · Cited by 1
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
Petrovic, I., Desai, S., Isaikina, P., Abiko, L. A., Spang, A., & Grzesiek, S. (2026) · eLife · doi:10.7554/elife.106839.4
Mostert, T. P., Kessler, A. L., Luijten, R. J., Doelman, W., Isendoorn, M. M. E., Filippov, D. V., van Kasteren, S. I., & Buschow, S. I. (2026) · The Journal of Immunology · doi:10.1093/jimmun/vkaf312
(2023) · doi:10.1101/2023.02.27.530196
Medwig-Kinney, T. N., Kinney, B. A., Martinez, M. A. Q., Yee, C., Sirota, S. S., Mullarkey, A. A., Somineni, N., Hippler, J., Zhang, W., Shen, K., et al. (2023) · doi:10.7554/elife.84355.2
Metadata
- Authors
- BOLTE, S., & CORDELIÈRES, F. P.
- Venue
- Journal of Microscopy
- Publisher
- Wiley
- Published
- 2006-12
- Volume
- 224
- Issue
- 3
- Pages
- 213-232
- ISSN
- 0022-2720 (ISSN-L)
- 1365-2818
- OpenAlex
- W2124733101
- Cited by
- 5,324
- References
- 0
- FWCI
- 23.89
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.