The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning
Open accessAbstract
Late endosomes (LEs) have characteristic intracellular distributions determined by their interactions with various motor proteins. Motor proteins associated to the dynactin subunit p150Glued bind to LEs via the Rab7 effector Rab7-interacting lysosomal protein (RILP) in association with the oxysterol-binding protein ORP1L. We found that cholesterol levels in LEs are sensed by ORP1L and are lower in peripheral vesicles. Under low cholesterol conditions, ORP1L conformation induces the formation of endoplasmic reticulum (ER)–LE membrane contact sites. At these sites, the ER protein VAP (VAMP [vesicle-associated membrane protein]-associated ER protein) can interact in trans with the Rab7–RILP complex to remove p150Glued and associated motors. LEs then move to the microtubule plus end. Under high cholesterol conditions, as in Niemann-Pick type C disease, this process is prevented, and LEs accumulate at the microtubule minus end as the result of dynein motor activity. These data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells.
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
Cites
Jordens, I., Fernandez-Borja, M., Marsman, M., Dusseljee, S., Janssen, L., Calafat, J., Janssen, H., Wubbolts, R., & Neefjes, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00531-0 · Cited by 811
Self-citationJohansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505
Self-citationHamilton, J. A. (2003) · Current Opinion in Lipidology · doi:10.1097/00041433-200306000-00006 · Cited by 184
Cited by
Shedding light on the cell biology of extracellular vesicles
van Niel, G., D'Angelo, G., & Raposo, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.125 · Cited by 8,369
Towards a systems understanding of MHC class I and MHC class II antigen presentation
Neefjes, J., Jongsma, M. L. M., Paul, P., & Bakke, O. (2011) · Nature Reviews Immunology · doi:10.1038/nri3084 · Cited by 2,044
Self-citationLysosomes as dynamic regulators of cell and organismal homeostasis
Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469
Structure and function of ER membrane contact sites with other organelles
Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933
The lysosome as a cellular centre for signalling, metabolism and quality control
Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586
Mechanisms and functions of lysosome positioning
Pu, J., Guardia, C. M., Keren-Kaplan, T., & Bonifacino, J. S. (2016) · Journal of Cell Science · doi:10.1242/jcs.196287 · Cited by 570
Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes
Wong, L. H., Gatta, A. T., & Levine, T. P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0071-5 · Cited by 505
Phosphoinositides as membrane organizers
Posor, Y., Jang, W., & Haucke, V. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00490-x · Cited by 469
A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
Hammond, G. R. V., Machner, M. P., & Balla, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312072 · Cited by 453
Organization and Function of Membrane Contact Sites
Helle, S. C. J., Kanfer, G., Kolar, K., Lang, A., Michel, A. H., & Kornmann, B. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.028 · Cited by 453
Cholesterol, the central lipid of mammalian cells
Maxfield, F. R., & van Meer, G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.05.004 · Cited by 414
Dong, R., Saheki, Y., Swarup, S., Lucast, L., Harper, J. W., & De Camilli, P. (2016) · Cell · doi:10.1016/j.cell.2016.06.037 · Cited by 398
ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
Friedman, J. R., Webster, B. M., Mastronarde, D. N., Verhey, K. J., & Voeltz, G. K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911024 · Cited by 393
A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387
Regulation of exosome production and cargo sorting
Wei, H., Chen, Q., Lin, L., Sha, C., Li, T., Liu, Y., Yin, X., Xu, Y., Chen, L., Gao, W., et al. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.53671 · Cited by 385
Lőrincz, P., & Juhász, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.028 · Cited by 328
NPC1 regulates ER contacts with endocytic organelles to mediate cholesterol egress
Höglinger, D., Burgoyne, T., Sanchez-Heras, E., Hartwig, P., Colaco, A., Newton, J., Futter, C. E., Spiegel, S., Platt, F. M., & Eden, E. R. (2019) · Nature Communications · doi:10.1038/s41467-019-12152-2 · Cited by 299
VAPs and ACBD5 tether peroxisomes to the ER for peroxisome maintenance and lipid homeostasis.
Hua, R., Cheng, D., Coyaud, É., Freeman, S., Di Pietro, E., Wang, Y., Vissa, A., Yip, C. M., Fairn, G. D., Braverman, N., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201608128 · Cited by 279
Moving and positioning the endolysosomal system
Bonifacino, J. S., & Neefjes, J. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.008 · Cited by 253
Self-citationA new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport
Gatta, A. T., Wong, L. H., Sere, Y. Y., Calderón-Noreña, D. M., Cockcroft, S., Menon, A. K., & Levine, T. P. (2015) · eLife · doi:10.7554/elife.07253 · Cited by 251
Staying in Touch: The Molecular Era of Organelle Contact Sites
Elbaz, Y., & Schuldiner, M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.08.004 · Cited by 226
Endoplasmic reticulum: ER stress regulates mitochondrial bioenergetics
Bravo, R., Gutierrez, T., Paredes, F., Gatica, D., Rodriguez, A. E., Pedrozo, Z., Chiong, M., Parra, V., Quest, A. F. G., Rothermel, B. A., et al. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.10.012 · Cited by 191
Lee, C. Y. D., Tse, W., Smith, J. D., & Landreth, G. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.295451 · Cited by 178
“Although the underlying reason why GDI extraction of Rab7 is modulated by cholesterol is unknown, results from previous studies suggested that this regulation perhaps involves oxysterol-binding protein-related protein 1L through the Rab7 effector Rab7-interacting lysosomal protein (35, 86, 87).”
BackgroundBorchers, A.-C., Langemeyer, L., & Ungermann, C. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202105120 · Cited by 181
Zhao, K., & Ridgway, N. D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.028 · Cited by 155
Lysosomal Exocytosis: The Extracellular Role of an Intracellular Organelle
Tancini, B., Buratta, S., Delo, F., Sagini, K., Chiaradia, E., Pellegrino, R. M., Emiliani, C., & Urbanelli, L. (2020) · Membranes · doi:10.3390/membranes10120406 · Cited by 144
Toops, K. A., Tan, L. X., Jiang, Z., Radu, R. A., & Lakkaraju, A. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-1028 · Cited by 105
Nonvesicular Lipid Transfer from the Endoplasmic Reticulum
Lev, S. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013300 · Cited by 103
Starling, G. P., Yip, Y. Y., Sanger, A., Morton, P. E., Eden, E. R., & Dodding, M. P. (2016) · The EMBO Reports · doi:10.15252/embr.201541382 · Cited by 96
Hao, F., Kondo, K., Itoh, T., Ikari, S., Nada, S., Okada, M., & Noda, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.208017 · Cited by 91
RUFY3 and RUFY4 are ARL8 effectors that promote coupling of endolysosomes to dynein-dynactin
Keren-Kaplan, T., Sarić, A., Ghosh, S., Williamson, C. D., Jia, R., Li, Y., & Bonifacino, J. S. (2022) · Nature Communications · doi:10.1038/s41467-022-28952-y · Cited by 79
ER – lysosome contacts at a pre-axonal region regulate axonal lysosome availability
Özkan, N., Koppers, M., van Soest, I., van Harten, A., Jurriens, D., Liv, N., Klumperman, J., Kapitein, L. C., Hoogenraad, C. C., & Farías, G. G. (2021) · Nature Communications · doi:10.1038/s41467-021-24713-5 · Cited by 69
Multiple sclerosis-associated CLEC16A controls HLA class II expression via late endosome biogenesis
van Luijn, M. M., Kreft, K. L., Jongsma, M. L., Mes, S. W., Wierenga-Wolf, A. F., van Meurs, M., Melief, M.-J., der Kant, R. V., Janssen, L., Janssen, H., et al. (2015) · Brain · doi:10.1093/brain/awv080 · Cited by 68
Self-citationProtective responses to sublytic complement in the retinal pigment epithelium
Tan, L. X., Toops, K. A., & Lakkaraju, A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523061113 · Cited by 66
The endolysosomal system in conventional and unconventional protein secretion
Néel, E., Chiritoiu-Butnaru, M., Fargues, W., Denus, M., Colladant, M., Filaquier, A., Stewart, S. E., Lehmann, S., Zurzolo, C., Rubinsztein, D. C., et al. (2024) · Journal of Cell Biology · doi:10.1083/jcb.202404152 · Cited by 50
Esteve-Rudd, J., Hazim, R. A., Diemer, T., Paniagua, A. E., Volland, S., Umapathy, A., & Williams, D. S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709211115 · Cited by 42
Cremer, T., Voortman, L. M., Bos, E., Jongsma, M. L., ter Haar, L. R., Akkermans, J. J., Talavera Ormeño, C. M., Wijdeven, R. H., de Vries, J., Kim, R. Q., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022111252 · Cited by 35
Self-citationSasazawa, Y., Souma, S., Furuya, N., Miura, Y., Kazuno, S., Kakuta, S., Suzuki, A., Hashimoto, R., Hirawake‐Mogi, H., Date, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022111476 · Cited by 31
Sensing of nutrients by CPT1C regulates late endosome/lysosome anterograde transport and axon growth
Palomo-Guerrero, M., Fadó, R., Casas, M., Pérez-Montero, M., Baena, M., Helmer, P. O., Domínguez, J. L., Roig, A., Serra, D., Hayen, H., et al. (2019) · eLife · doi:10.7554/elife.51063 · Cited by 30
ER–endosome contact sites in endosome positioning and protrusion outgrowth
Raiborg, C., Wenzel, E. M., Pedersen, N. M., & Stenmark, H. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150246 · Cited by 29
DENN domain-containing protein FAM45A regulates the homeostasis of late/multivesicular endosomes
Zhang, J., Zhang, K., Qi, L., Hu, Q., Shen, Z., Liu, B., Deng, J., Zhang, C., & Zhang, Y. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.02.006 · Cited by 29
Ramachandra Rao, S., Pfeffer, B. A., Más Gómez, N., Skelton, L. A., Keiko, U., Sparrow, J. R., Rowsam, A. M., Mitchell, C. H., & Fliesler, S. J. (2018) · Autophagy · doi:10.1080/15548627.2018.1490851 · Cited by 28
RNF13 mediates pH- and Ca2+-dependent regulation of lysosomal positioning
Trinh, L. T., Van Vu, A., Shin, S., Lee, C., Park, S.-H., Cho, E.-B., Heo, Y., Kim, H. J., Kim, S., & Yoon, J.-B. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116053 · Cited by 7
Regulation of lysosomal positioning via TMEM55B phosphorylation
Araki, M., & Kontani, K. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab013 · Cited by 7
Metadata
- Authors
- Rocha, N., Kuijl, C., van der Kant, R., Janssen, L., Houben, D., Janssen, H., Zwart, W., & Neefjes, J.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2009-06-29
- Volume
- 185
- Issue
- 7
- Pages
- 1209-1225
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2160975493
- Cited by
- 702
- References
- 3
- FWCI
- 10.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
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.
