Bibliography
Guo, Q., Lehmer, C., MartÃnez-Sánchez, A., Rudack, T., Beck, F., Hartmann, H., Pérez-Berlanga, M., Frottin, F., Hipp, M. S., Hartl, F. U., Edbauer, D., Baumeister, W., & Fernández-Busnadiego, R. (2018). In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment. Cell, 172(4), 696-705.e12.
Authors
13
- Qiang Guo (first)
- Carina Lehmer (additional)
- Antonio Martínez-Sánchez (additional)
- Till Rudack (additional)
- Florian Beck (additional)
- Hannelore Hartmann (additional)
- Manuela Pérez-Berlanga (additional)
- Frédéric Frottin (additional)
- Mark S. Hipp (additional)
- F. Ulrich Hartl (additional)
- Dieter Edbauer (additional)
- Wolfgang Baumeister (additional)
- Rubén Fernández-Busnadiego (additional)
References
94
Referenced
351
10.1126/science.1261197
/ Science / Proteasomes. A molecular census of 26S proteasomes in intact neurons by Asano (2015)10.1016/j.neuron.2013.02.004
/ Neuron / Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS by Ash (2013)10.1073/pnas.1510449112
/ Proc. Natl. Acad. Sci. USA / Structural characterization of the interaction of Ubp6 with the 26S proteasome by Aufderheide (2015)10.1038/nsmb.3075
/ Nat. Struct. Mol. Biol. / Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome by Bashore (2015)10.1016/j.cell.2017.08.009
/ Cell / In situ architecture and cellular interactions of polyQ inclusions by Bauerlein (2017)10.1016/j.tcb.2016.08.006
/ Trends Cell Biol. / Cryo-electron tomography: can it reveal the molecular sociology of cells in atomic detail? by Beck (2016)10.1016/j.molcel.2004.12.021
/ Mol. Cell / Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation by Bennett (2005)10.1038/nprot.2016.124
/ Nat. Protoc. / Resolving macromolecular structures from electron cryo-tomography data using subtomogram averaging in RELION by Bharat (2016)10.1074/jbc.M115.694273
/ J. Biol. Chem. / The glycine-alanine dipeptide repeat from C9orf72 hexanucleotide expansions forms toxic amyloids possessing cell-to-cell transmission properties by Chang (2016)10.1073/pnas.1614614113
/ Proc. Natl. Acad. Sci. USA / Structural basis for dynamic regulation of the human 26S proteasome by Chen (2016)10.1016/j.str.2016.05.018
/ Structure / Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding mechanisms between substrate receptors and shuttle factors of the proteasome by Chen (2016)10.1093/hmg/ddn319
/ Hum. Mol. Genet. / Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis by Cheroni (2009)10.1016/j.cell.2017.04.023
/ Cell / The logic of the 26S proteasome by Collins (2017)10.3389/fnmol.2014.00070
/ Front. Mol. Neurosci. / The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution by Dantuma (2014)10.1038/75406
/ Nat. Biotechnol. / Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells by Dantuma (2000)10.1002/path.4872
/ J. Pathol. / Nuclear inclusion bodies of mutant and wild-type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation by De Smet (2017)10.1016/j.neuron.2011.09.011
/ Neuron / Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS by DeJesus-Hernandez (2011)10.1038/nature10353
/ Nature / Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia by Deng (2011)10.1038/emboj.2011.224
/ EMBO J. / Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entry by Deriziotis (2011)10.1016/j.conb.2015.10.009
/ Curr. Opin. Neurobiol. / An amyloid-like cascade hypothesis for C9orf72 ALS/FTD by Edbauer (2016)10.1038/ncb845
/ Nat. Cell Biol. / Proteasome subunit Rpn1 binds ubiquitin-like protein domains by Elsasser (2002)10.1016/j.bpj.2015.10.043
/ Biophys. J. / Removing contamination-induced reconstruction artifacts from cryo-electron tomograms by Fernandez (2016)10.1016/j.tibs.2015.10.009
/ Trends Biochem. Sci. / Gates, channels, and switches: Elements of the [proteasome machine by Finley (2016)10.3389/fnmol.2017.00035
/ Front. Mol. Neurosci. / The role of dipeptide repeats in C9ORF72-related ALS-FTD by Freibaum (2017){'key': '10.1016/j.cell.2017.12.030_bib25', 'first-page': 'a024224', 'article-title': 'Disease mechanisms of C9ORF72 repeat expansions', 'author': 'Gendron', 'year': '2017', 'journal-title': 'Cold Spring Harb. Perspect. Med.'}
/ Cold Spring Harb. Perspect. Med. / Disease mechanisms of C9ORF72 repeat expansions by Gendron (2017)10.1007/s00401-013-1192-8
/ Acta Neuropathol. / Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeat-associated non-ATG translation in c9FTD/ALS by Gendron (2013)10.1146/annurev-biophys-062215-011113
/ Annu. Rev. Biophys. / Computational methodologies for real-space structural refinement of large macromolecular complexes by Goh (2016)10.1038/80384
/ Nat. Med. / Basic medical research award. The ubiquitin system by Hershko (2000)10.1007/978-1-61779-474-2_33
/ Methods Mol. Biol. / Live-cell imaging of ubiquitin-proteasome system function by Hipp (2012)10.1083/jcb.201110093
/ J. Cell Biol. / Indirect inhibition of 26S proteasome activity in a cellular model of Huntington’s disease by Hipp (2012)10.1016/j.tcb.2014.05.003
/ Trends Cell Biol. / Proteostasis impairment in protein-misfolding and -aggregation diseases by Hipp (2014)10.1074/jbc.274.39.28019
/ J. Biol. Chem. / Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome by Hiyama (1999)10.1016/j.cell.2016.07.001
/ Cell / UBQLN2 mediates autophagy-independent protein aggregate clearance by the proteasome by Hjerpe (2016)10.1038/sj.emboj.7601058
/ EMBO J. / Glycine-alanine repeats impair proper substrate unfolding by the proteasome by Hoyt (2006)10.1016/j.jsb.2011.12.003
/ J. Struct. Biol. / PyTom: a python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis by Hrabe (2012)10.1038/nsmb.3273
/ Nat. Struct. Mol. Biol. / An atomic structure of the human 26S proteasome by Huang (2016)10.1016/0263-7855(96)00018-5
/ J. Mol. Graph. / VMD: visual molecular dynamics by Humphrey (1996)10.1016/j.neuron.2010.11.036
/ Neuron / Exome sequencing reveals VCP mutations as a cause of familial ALS by Johnson (2010)10.1038/nn.4085
/ Nat. Neurosci. / Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS by Jovičić (2015)10.1038/nature14427
/ Nature / Structure of the human 80S ribosome by Khatter (2015)10.1038/nsmb1335
/ Nat. Struct. Mol. Biol. / Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites by Kleijnen (2007)10.1038/nrm3810
/ Nat. Rev. Mol. Cell Biol. / The amyloid state and its association with protein misfolding diseases by Knowles (2014)10.1074/jbc.M113.512533
/ J. Biol. Chem. / Slippery substrates impair ATP-dependent protease function by slowing unfolding by Kraut (2013)10.1006/jsbi.1996.0013
/ J. Struct. Biol. / Computer visualization of three-dimensional image data using IMOD by Kremer (1996)10.1038/emboj.2010.167
/ EMBO J. / ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons by Kuhn (2010)10.1016/j.celrep.2013.10.049
/ Cell Rep. / Hexanucleotide repeats in ALS/FTD form length-dependent RNA foci, sequester RNA binding proteins, and are neurotoxic by Lee (2013)10.1016/S1097-2765(02)00638-X
/ Mol. Cell / Multiple associated proteins regulate proteasome structure and function by Leggett (2002)10.1016/j.str.2012.03.007
/ Structure / The molecular architecture of the eukaryotic chaperonin TRiC/CCT by Leitner (2012)10.1073/pnas.94.23.12616
/ Proc. Natl. Acad. Sci. USA / Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1 by Levitskaya (1997)10.1038/nmeth.2472
/ Nat. Methods / Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM by Li (2013)10.1016/bs.ctdb.2016.07.004
/ Curr. Top. Dev. Biol. / Amyotrophic lateral sclerosis pathogenesis converges on defects in protein homeostasis associated with TDP-43 mislocalization and proteasome-mediated degradation overload by Lin (2017)10.1126/science.1250834
/ Science / Substrate degradation by the proteasome: a single-molecule kinetic analysis by Lu (2015)10.1016/j.str.2005.02.005
/ Structure / Morphological characterization of molecular complexes present in the synaptic cleft by Lucić (2005)10.1007/s00401-013-1181-y
/ Acta Neuropathol. / Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations by Mackenzie (2013)10.1007/s00401-015-1476-2
/ Acta Neuropathol. / Quantitative analysis and clinico-pathological correlations of different dipeptide repeat protein pathologies in C9ORF72 mutation carriers by Mackenzie (2015)10.1016/S1474-4422(12)70043-1
/ Lancet Neurol. / Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study by Majounie (2012)10.1016/j.jsb.2014.02.015
/ J. Struct. Biol. / Robust membrane detection based on tensor voting for electron tomography by Martinez-Sanchez (2014)10.1016/j.jsb.2005.07.007
/ J. Struct. Biol. / Automated electron microscope tomography using robust prediction of specimen movements by Mastronarde (2005)10.1007/s00401-014-1329-4
/ Acta Neuropathol. / C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration by May (2014)10.1007/s00401-013-1189-3
/ Acta Neuropathol. / Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins by Mori (2013)10.1126/science.1232927
/ Science / The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS by Mori (2013)10.1093/emboj/cdg467
/ EMBO J. / Structural determinants for the binding of ubiquitin-like domains to the proteasome by Mueller (2003)10.1038/nm.4011
/ Nat. Med. / Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling by Myeku (2016)10.1016/j.jsb.2004.10.006
/ J. Struct. Biol. / TOM software toolbox: acquisition and analysis for electron tomography by Nickell (2005)10.1016/j.cell.2010.11.050
/ Cell / Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions by Olzscha (2011)10.1016/j.cell.2013.06.003
/ Cell / PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone by Park (2013)10.1002/jcc.20084
/ J. Comput. Chem. / UCSF Chimera--a visualization system for exploratory research and analysis by Pettersen (2004)10.1002/jcc.20289
/ J. Comput. Chem. / Scalable molecular dynamics with NAMD by Phillips (2005)10.1016/j.neuron.2011.09.010
/ Neuron / A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD by Renton (2011)10.1038/srep26536
/ Sci. Rep. / QwikMD-Integrative molecular dynamics toolkit for novices and experts by Ribeiro (2016)10.1073/pnas.1201333109
/ Proc. Natl. Acad. Sci. USA / Focused ion beam micromachining of eukaryotic cells for cryoelectron tomography by Rigort (2012)10.1038/nmeth.2115
/ Nat. Methods / Prevention of overfitting in cryo-EM structure determination by Scheres (2012)10.1038/nmeth.2019
/ Nat. Methods / Fiji: an open-source platform for biological-image analysis by Schindelin (2012)10.1007/s00401-017-1711-0
/ Acta Neuropathol. / Spinal poly-GA inclusions in a C9orf72 mouse model trigger motor deficits and inflammation without neuron loss by Schludi (2017)10.1016/j.bbamcr.2013.08.012
/ Biochim. Biophys. Acta / Regulation of proteasome activity in health and disease by Schmidt (2014){'year': '2006', 'author': 'Schroeder', 'series-title': 'The Visualization Toolkit: an object-oriented approach to 3D graphics', 'key': '10.1016/j.cell.2017.12.030_bib76'}
/ The Visualization Toolkit: an object-oriented approach to 3D graphics by Schroeder (2006)10.1073/pnas.1608050113
/ Proc. Natl. Acad. Sci. USA / Structure of the human 26S proteasome at a resolution of 3.9 Å by Schweitzer (2016)10.1126/science.aad9421
/ Science / Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome by Shi (2016){'key': '10.1016/j.cell.2017.12.030_bib79', 'first-page': '12', 'article-title': 'Characterization of the brain 26S proteasome and its interacting proteins', 'volume': '3', 'author': 'Tai', 'year': '2010', 'journal-title': 'Front. Mol. Neurosci.'}
/ Front. Mol. Neurosci. / Characterization of the brain 26S proteasome and its interacting proteins by Tai (2010)10.1074/jbc.M112.417600
/ J. Biol. Chem. / Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis by Tashiro (2012)10.1017/S1431927608080781
/ Microsc. Microanal. / An improved cryogen for plunge freezing by Tivol (2008)10.1016/j.ymeth.2009.04.005
/ Methods / Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography by Trabuco (2009)10.1073/pnas.1403409111
/ Proc. Natl. Acad. Sci. USA / Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome by Unverdorben (2014)10.1002/humu.22244
/ Hum. Mutat. / A pan-European study of the C9orf72 repeat associated with FTLD: geographic prevalence, genomic instability, and intermediate repeats by van der Zee (2013)10.1091/mbc.12.5.1393
/ Mol. Biol. Cell / Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation by Waelter (2001)10.1021/bi011892y
/ Biochemistry / Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a by Walters (2002)10.1038/ng1332
/ Nat. Genet. / Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein by Watts (2004)10.1073/pnas.1621129114
/ Proc. Natl. Acad. Sci. USA / Structural insights into the functional cycle of the ATPase module of the 26S proteasome by Wehmer (2017)10.1093/hmg/ddu576
/ Hum. Mol. Genet. / Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS by Yamakawa (2015)10.1038/nsmb.3309
/ Nat. Struct. Mol. Biol. / Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM by Zang (2016)10.1007/s00401-014-1336-5
/ Acta Neuropathol. / Aggregation-prone c9FTD/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress by Zhang (2014)10.1038/nn.4272
/ Nat. Neurosci. / C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins by Zhang (2016)10.1073/pnas.1013343108
/ Proc. Natl. Acad. Sci. USA / Non-ATG-initiated translation directed by microsatellite expansions by Zu (2011)10.1073/pnas.1315438110
/ Proc. Natl. Acad. Sci. USA / RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia by Zu (2013)
Dates
Type | When |
---|---|
Created | 7 years, 6 months ago (Feb. 1, 2018, 1:22 p.m.) |
Deposited | 5 years, 2 months ago (May 25, 2020, 12:08 a.m.) |
Indexed | 1 day, 16 hours ago (Aug. 20, 2025, 8:37 a.m.) |
Issued | 7 years, 6 months ago (Feb. 1, 2018) |
Published | 7 years, 6 months ago (Feb. 1, 2018) |
Published Print | 7 years, 6 months ago (Feb. 1, 2018) |
Funders
9
EMBO
10.13039/501100003043
Awards
1
- EMBO ALTF 73-2015
Alexander von Humboldt Foundation
10.13039/100005156
Alexander von Humboldt-StiftungRegion: Europe
pri (Trusts, charities, foundations (both public and private))
Labels
5
- Humboldt-Stiftung
- Humboldt Foundation
- Alexander von Humboldt Foundation
- Humboldt Stiftung
- AvH
Séneca Foundation
10.13039/100007801
Fundación SénecaRegion: Europe
pri (Trusts, charities, foundations (both public and private))
Labels
5
- Séneca Foundation
- Séneca Foundation - Agency of Science and Technology of the Region of Murcia
- Fundación Séneca, Agencia Regional de Ciencia y Tecnología
- Fundación Séneca - Agencia de Ciencia y Tecnología de la Región de Murcia
- FS
European Commission
10.13039/501100000780
Region: Europe
gov (National government)
Labels
26
- European Union
- Comisión Europea
- Europäische Kommission
- EU-Kommissionen
- Euroopa Komisjoni
- Ευρωπαϊκής Επιτροπής
- Европейската комисия
- Evropské komise
- Commission européenne
- Choimisiúin Eorpaigh
- Europskoj komisiji
- Commissione europea
- La Commissione europea
- Eiropas Komisiju
- Europos Komisijos
- Európai Bizottságról
- Europese Commissie
- Komisja Europejska
- Comissão Europeia
- Comisia Europeană
- Európskej komisii
- Evropski komisiji
- Euroopan komission
- Europeiska kommissionen
- EC
- EU
Awards
2
- FP7 GA ERC-2012-SyG_318987–ToPAG
- FP7 GA ERC-2013-CoG_617198 DPR-MODELS
German Science Foundation
Munich Cluster for Systems Neurology
Awards
1
- SFB-1035/Project A01
NOMIS Foundation
10.13039/501100008483
NOMIS StiftungRegion: Europe
pri (Trusts, charities, foundations (both public and private))
Labels
1
- NOMIS Foundation
Helmholtz Association
10.13039/501100001656
Helmholtz-GemeinschaftRegion: Europe
pri (Associations and societies (private and public))
Labels
4
- Helmholtz Association
- Helmholtz Association of German Research Centres
- Helmholtz Gemeinschaft
- HGF
NIH
10.13039/100000002
National Institutes of HealthRegion: Americas
gov (National government)
Labels
3
- Institutos Nacionales de la Salud
- US National Institutes of Health
- NIH
Awards
1
- 9P41GM10460
@article{Guo_2018, title={In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment}, volume={172}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/j.cell.2017.12.030}, DOI={10.1016/j.cell.2017.12.030}, number={4}, journal={Cell}, publisher={Elsevier BV}, author={Guo, Qiang and Lehmer, Carina and Martínez-Sánchez, Antonio and Rudack, Till and Beck, Florian and Hartmann, Hannelore and Pérez-Berlanga, Manuela and Frottin, Frédéric and Hipp, Mark S. and Hartl, F. Ulrich and Edbauer, Dieter and Baumeister, Wolfgang and Fernández-Busnadiego, Rubén}, year={2018}, month=feb, pages={696-705.e12} }