The DOI matches its Crossref record; 60 of the 61 references it cites were found in a registry or an index.
Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling
Abstract
Structure of human mTORC1 components: The mTORC1 (mechanistic target of rapamycin complex 1) complex garners much attention as a signaling hub that coordinates input from growth-factor receptors and nutrient availability with metabolism and cell growth and proliferation. de Araujo et al. report the crystal structure of the LAMTOR (or “Ragulator”) complex that helps assemble mTORC1 at the lysosomal membrane for activation. The structure and functional studies reveal how LAMTOR1 wraps around the other subunits to hold them in place and interacts with the Rag guanosine triphosphatases in the complex. Science , this issue p. 377
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The heptameric Ragulator-Rag complex structure showed Rag C-terminal roadblock domains binding to the LAMTOR2-LAMTOR3 heterodimer (de Araujo et al., 2017; Su et al., 2017; Yonehara et al., 2017) (Fig. 4B), thus building a tower of three roadblock domain-mediated heterodimers tied together by the extended LAMTOR1 subunit, and presenting the GTPase domains for interaction with RAPTOR.”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as de Araujo et al., 2017
In the citing paper
“It is important to note that when the Rag heterodimer binds Ragulator, the N-terminal portion of LAMTOR1 encompassing residues 47-64 is resolved, forming an α-helix which packs against the RagC roadblock domain, whereas in the Ragulator complex alone this region of LAMTOR1 was disordered (de Araujo et al., 2017; Yonehara et al., 2017).”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as de Araujo et al., 2017
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007
Universal sample preparation method for proteome analysis
Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352
Towards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511
Improved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239
Genome-scale CRISPR-Cas9 knockout screening in human cells
Shalem, O., Sanjana, N. E., Hartenian, E., Shi, X., Scott, D. A., Mikkelsen, T. S., Heckl, D., Ebert, B. L., Root, D. E., Doench, J. G., et al. (2014) · Science · doi:10.1126/science.1247005 · Cited by 5,234
MOLREP : an Automated Program for Molecular Replacement
Vagin, A. A., & Teplyakov, A. (1997) · Journal of Applied Crystallography · doi:10.1107/s0021889897006766 · Cited by 4,756
DNA targeting specificity of RNA-guided Cas9 nucleases
Hsu, P. D., Scott, D. A., Weinstein, J. A., Ran, F. A., Konermann, S., Agarwala, V., Li, Y., Fine, E. J., Wu, X., Shalem, O., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2647 · Cited by 4,741
Assay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464
The Buccaneer software for automated model building. 1. Tracing protein chains
Cowtan, K. D. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906022116 · Cited by 1,834
Identification and characterization of essential genes in the human genome
Wang, T., Birsoy, K., Hughes, N. W., Krupczak, K. M., Post, Y., Wei, J. J., Lander, E. S., & Sabatini, D. M. (2015) · Science · doi:10.1126/science.aac7041 · Cited by 1,617
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
Langer, G., Cohen, S. X., Lamzin, V. S., & Perrakis, A. (2008) · Nature Protocols · doi:10.1038/nprot.2008.91 · Cited by 1,606
Ragulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1
Bar-Peled, L., Schweitzer, L. D., Zoncu, R., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.07.032 · Cited by 918
Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
Wang, S., Tsun, Z.-Y., Wolfson, R. L., Shen, K., Wyant, G. A., Plovanich, M., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 865
Gene essentiality and synthetic lethality in haploid human cells
Blomen, V. A., Májek, P., Jae, L. T., Bigenzahn, J. W., Nieuwenhuis, J., Staring, J., Sacco, R., van Diemen, F. R., Olk, N., Stukalov, A., et al. (2015) · Science · doi:10.1126/science.aac7557 · Cited by 857
Regulation of mTORC1 by amino acids
Bar-Peled, L., & Sabatini, D. M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.003 · Cited by 773
SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673
Self-citationControlled expression of transgenes introduced by in vivo electroporation
Matsuda, T., & Cepko, C. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610155104 · Cited by 666
The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway
Wolfson, R. L., & Sabatini, D. M. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.001 · Cited by 563
CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
Stein, N. (2008) · Journal of Applied Crystallography · doi:10.1107/s0021889808006985 · Cited by 536
BORC, a Multisubunit Complex that Regulates Lysosome Positioning
Pu, J., Schindler, C., Jia, R., Jarnik, M., Backlund, P., & Bonifacino, J. S. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.011 · Cited by 406
Teis, D., Wunderlich, W., & Huber, L. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00364-7 · Cited by 371
Self-citationStavroX—A Software for Analyzing Crosslinked Products in Protein Interaction Studies
Götze, M., Pettelkau, J., Schaks, S., Bosse, K., Ihling, C. H., Krauth, F., Fritzsche, R., Kühn, U., & Sinz, A. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-011-0261-2 · Cited by 345
Nada, S., Hondo, A., Kasai, A., Koike, M., Saito, K., Uchiyama, Y., & Okada, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.308 · Cited by 341
Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9
Jung, J., Genau, H. M., & Behrends, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00125-15 · Cited by 266
Low-resolution refinement tools in REFMAC5
Nicholls, R. A., Long, F., & Murshudov, G. N. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744491105606x · Cited by 244
Cost, G. J., & Boeke, J. D. (1998) · Biochemistry · doi:10.1021/bi981858s · Cited by 242
The Protein Interaction Landscape of the Human CMGC Kinase Group
Varjosalo, M. T., Keskitalo, S., van Drogen, A., Nurkkala, H., Vichalkovski, A., Aebersold, R. H., & Gstaiger, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.027 · Cited by 235
Gabadinho, J., Beteva, A., Guijarro, M., Rey‐Bakaikoa, V., Spruce, D., Bowler, M. W., Brockhauser, S., Flot, D. M., Gordon, E. J., Hall, D. R., et al. (2010) · Journal of Synchrotron Radiation · doi:10.1107/s0909049510020005 · Cited by 230
Teis, D., Taub, N., Kurzbauer, R., Hilber, D., de Araujo, M. E. G., Erlacher, M., Offterdinger, M., Villunger, A., Geley, S., Bohn, G., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200607025 · Cited by 214
Self-citationImproved low-resolution crystallographic refinement with Phenix and Rosetta
DiMaio, F., Echols, N., Headd, J. J., Terwilliger, T. C., Adams, P. D., & Baker, D. A. (2013) · Nature Methods · doi:10.1038/nmeth.2648 · Cited by 183
Dynamics of mTORC1 activation in response to amino acids
Manifava, M., Smith, M. D., Rotondo, S., Walker, S. A., Niewczas, I. S., Zoncu, R., Clark, J. P., & Ktistakis, N. T. (2016) · eLife · doi:10.7554/elife.19960 · Cited by 123
A PCR Based Protocol for Detecting Indel Mutations Induced by TALENs and CRISPR/Cas9 in Zebrafish
Yu, C., Zhang, Y., Yao, S., & Wei, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098282 · Cited by 102
Vijayachandran, L. S., Viola, C., Garzoni, F., Trowitzsch, S., Bieniossek, C., Chaillet, M., Schaffitzel, C., Busso, D., Romier, C., Poterszman, A., et al. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.03.007 · Cited by 99
Gong, R., Li, L., Liu, Y., Wang, P., Yang, H., Wang, L., Cheng, J., Guan, K.-L., & Xu, Y. (2011) · Genes & Development · doi:10.1101/gad.16968011 · Cited by 98
Schiefermeier-Mach, N., Scheffler, J. M., de Araújo, M. E. G., Stasyk, T., Yordanov, T. E., Ebner, H. L., Offterdinger, M., Munck, S., Hess, M. W., Wickström, S. A., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201310043 · Cited by 95
Self-citationKurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403435101 · Cited by 95
Self-citationPowis, K., Zhang, T., Panchaud, N., Wang, R., Virgilio, C. D., & Ding, J. (2015) · Cell Research · doi:10.1038/cr.2015.86 · Cited by 80
Dynamic relocation of the TORC1–Gtr1/2–Ego1/2/3 complex is regulated by Gtr1 and Gtr2
Kira, S., Kumano, Y., Ukai, H., Takeda, E., Matsuura, A., & Noda, T. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-07-0470 · Cited by 77
Jeong, J.-H., Lee, K.-H., Kim, Y.-M., Kim, D.-H., Oh, B.-H., & Kim, Y.-G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.384420 · Cited by 68
The Structure of the MAPK Scaffold, MP1, Bound to Its Partner, p14
Lunin, V. V., Munger, C., Wagner, J., Ye, Z., Cygler, M., & Sacher, M. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401648200 · Cited by 67
Zhang, T., Gulli, M., Yang, H., VIRGILIO, C. D., & Ding, J. (2012) · Structure · doi:10.1016/j.str.2012.09.019 · Cited by 63
LAMTOR2 regulates dendritic cell homeostasis through FLT3-dependent mTOR signalling
Scheffler, J. M., Sparber, F., Tripp, C. H., Herrmann, C., Humenberger, A., Blitz, J., Romani, N., Stoitzner, P., & Huber, L. A. (2014) · Nature Communications · doi:10.1038/ncomms6138 · Cited by 46
Self-citationThe late endosome/lysosome-anchored p18-mTORC1 pathway controls terminal maturation of lysosomes
Takahashi, Y., Nada, S., Mori, S., Soma‐Nagae, T., Oneyama, C., & Okada, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.12.082 · Cited by 44
Hall, J., Song, Y., Karplus, P. A., & Barbar, E. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.103861 · Cited by 41
Disruption of the Rag-Ragulator Complex by c17orf59 Inhibits mTORC1
Schweitzer, L. D., Comb, W. C., Bar‐Peled, L., & Sabatini, D. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.052 · Cited by 36
The MultiBac Protein Complex Production Platform at the EMBL
Berger, I., Garzoni, F., Chaillet, M., Haffke, M., Gupta, K., & Aubert, A. (2013) · Journal of Visualized Experiments · doi:10.3791/50159 · Cited by 36
Garcia-Saez, I., Lacroix, F., Blot, D., Gabel, F., & Skoufias, D. A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.046 · Cited by 36
de Araújo, M. E. G., Stasyk, T., Taub, N., Ebner, H. L., Fürst, B., Filipek, P. A., Weys, S., Hess, M. W., Lindner, H., Kremser, L., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349480 · Cited by 36
Self-citationTaub, N., Nairz, M., Hilber, D., Hess, M. W., Weiß, G., & Huber, L. A. (2012) · Journal of Cell Science · doi:10.1242/jcs.100073 · Cited by 28
Self-citationLAMTOR1 depletion induces p53-dependent apoptosis via aberrant lysosomal activation
Malek, M., Guillaumot, P., Huber, A.-L., Lebeau, J., Pétrilli, V., Kfoury, A., Mikaélian, I., Renno, T., & Manié, S. N. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.39 · Cited by 24
Interactions between Kinase Scaffold MP1/p14 and Its Endosomal Anchoring Protein p18
Magee, J., & Cygler, M. (2011) · Biochemistry · doi:10.1021/bi101972y · Cited by 23
Flagged first, then by citations
1 of the 61 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Lysosomes 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
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
Targeting mTOR for cancer therapy
Hua, H. M., Kong, Q., Zhang, H., Wang, J., Luo, T. L., & Jiang, Y. (2019) · Journal of Hematology & Oncology · doi:10.1186/s13045-019-0754-1 · Cited by 929
A substrate-specific mTORC1 pathway underlies Birt–Hogg–Dubé syndrome
Napolitano, G., Di Malta, C., Esposito, A., de Araujo, M. E. G., Pece, S., Bertalot, G., Matarese, M., Benedetti, V., Zampelli, A., Stasyk, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2444-0 · Cited by 341
Self-citationNutrient regulation of mTORC1 at a glance
Condon, K. J., & Sabatini, D. M. (2019) · Journal of Cell Science · doi:10.1242/jcs.222570 · Cited by 342
Metadata
- Authors
- de Araujo, M. E. G., Naschberger, A., Fürnrohr, B. G., Stasyk, T., Dunzendorfer-Matt, T., Lechner, S., Welti, S., Kremser, L., Shivalingaiah, G., Offterdinger, M., Lindner, H. H., Huber, L. A., & Scheffzek, K.
- Affiliations
- Division of Cell Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
- Innsbruck Medical University (AT)
- Corresponding author
- Naschberger, Andreas
- Fürnrohr, Barbara G.
- Huber, Lukas A.
- Scheffzek, Klaus
- ORCID
- Venue
- Science
- Published
- 2017-10-20
- Volume
- 358
- Issue
- 6361
- Pages
- 377-381
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2757150230
- Cited by
- 134
- References
- 61
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 13 · 2023: 11 · 2022: 20 · 2021: 14 · 2020: 15 · 2019: 19 · 2018: 9 · 2017: 9
- FWCI
- 5.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Austrian Science Fund (award337283, P26682, award337284, P28975)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- Ragulator complex, mTORC1, LAMTOR1, Rag GTPases, lysosomes, heterodimer assembly, mTOR signaling, crystal structure, protein complex formation
- MeSH terms
- Protein Domains, Mechanistic Target of Rapamycin Complex 1, Carrier Proteins, Humans, Lysosomes, Signal Transduction, Crystallography, X-Ray, GTP Phosphohydrolases, Intracellular Signaling Peptides and Proteins
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
