Cited by 339

The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.

Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6

Open access

Olzmann, James A., Li, Lian, Chudaev, Maksim V., Chen, Jue, Perez, Francisco A., Palmiter, Richard D., Chin, Lih-Shen·2007·The Journal of Cell Biology

DOI 10.1083/jcb.200611128

Open this paper in CoChat — free account

Abstract

Sequestration of misfolded proteins into pericentriolar inclusions called aggresomes is a means that cells use to minimize misfolded protein-induced cytotoxicity. However, the molecular mechanism by which misfolded proteins are recruited to aggresomes remains unclear. Mutations in the E3 ligase parkin cause autosomal recessive Parkinson's disease that is devoid of Lewy bodies, which are similar to aggresomes. Here, we report that parkin cooperates with heterodimeric E2 enzyme UbcH13/Uev1a to mediate K63-linked polyubiquitination of misfolded DJ-1. K63-linked polyubiquitination of misfolded DJ-1 serves as a signal for interaction with histone deacetylase 6, an adaptor protein that binds the dynein–dynactin complex. Through this interaction, misfolded DJ-1 is linked to the dynein motor and transported to aggresomes. Furthermore, fibroblasts lacking parkin display deficits in targeting misfolded DJ-1 to aggresomes. Our findings reveal a signaling role for K63-linked polyubiquitination in dynein-mediated transport, identify parkin as a key regulator in the recruitment of misfolded DJ-1 to aggresomes, and have important implications regarding the biogenesis of Lewy bodies.

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

Crossref · 10.1083/jcb.200611128

Cites

78 of 78 references verified0 citation errors · 0 not checkable

Statistics

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.

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism
Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibanez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,778
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N. F., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,187
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · cited 2×
“In vitro ubiquitination assays were performed using a well-established reconstitution system (Shimura et al., 2000, 2001; Pridgeon et al., 2003).”
Method
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,921
Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress
Kawaguchi, Y., Kovacs, J. J., McLaurin, A., Vance, J. M., Ito, A., & Yao, T.-P. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,524
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,482
Association between Early-Onset Parkinson's Disease and Mutations in the Parkin Gene
Lücking, C. B., Dürr, A., Bonifati, V., Vaughan, J., De Michele, G., Gasser, T., Harhangi, B. S., Meco, G., Denèfle, P., Wood, N. W., et al. (2000) · New England Journal of Medicine · doi:10.1056/nejm200005253422103 · Cited by 1,433
Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease
Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2001) · Science · doi:10.1126/science.1060627 · Cited by 1,053
Polyubiquitin chains: polymeric protein signals
Pickart, C. M., & Fushman, D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.09.009 · Cited by 1,049
Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
Zhang, Y., Gao, J., Chung, K. K. K., Huang, H., Dawson, V. L., & Dawson, T. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240347797 · Cited by 982
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913
Protein carbonylation, cellular dysfunction, and disease progression
Dalle-Donne, I., Aldini, G., Carini, M., Colombo, R., Rossi, R., & Milzani, A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00407.x · Cited by 831
Subversion of Cellular Autophagosomal Machinery by RNA Viruses
Jackson, W. T., Giddings, T. H., Taylor, M. P., Mulinyawe, S., Rabinovitch, M., Kopito, R. R., & Kirkegaard, K. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030156 · Cited by 818
Ubiquitylation and cell signaling
Haglund, K., & Dikic, I. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600808 · Cited by 734
HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin.
Iwata, A., Riley, B. E., Johnston, J. A., & Kopito, R. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508786200 · Cited by 719
Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles.
Biederbick, A., Kern, H., & Elsässer, H. (1995) · PubMed · Cited by 706
Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera✪
García-Mata, R., Bebök, Z., Sorscher, E. J., & Sztul, E. S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.6.1239 · Cited by 595
Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma
Hideshima, T., Bradner, J. E., Wong, J., Chauhan, D., Richardson, P., Schreiber, S. L., & Anderson, K. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503221102 · Cited by 593
DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation
Shendelman, S., Jonason, A., Martinat, C., Leete, T., & Abeliovich, A. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020362 · Cited by 590
Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease
Sulzer, D. (2007) · Trends in Neurosciences · doi:10.1016/j.tins.2007.03.009 · Cited by 587
A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting
Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523
Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation
Bennett, E. J., Bence, N. F., Jayakumar, R., & Kopito, R. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.021 · Cited by 509
Parkin Mediates Nonclassical, Proteasomal-Independent Ubiquitination of Synphilin-1: Implications for Lewy Body Formation
Lim, K. L., Chew, K. C. M., Tan, J. M. M., Wang, C., Chung, K. K. K., Zhang, Y., Tanaka, Y., Smith, W., Engelender, S., Ross, C. A., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4474-04.2005 · Cited by 503
Parkin-deficient mice are not a robust model of parkinsonism
Perez, F. A., & Palmiter, R. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409598102 · Cited by 477
Self-citation
CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase Activity
Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K.-I., & Takahashi, R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00583-x · Cited by 473
Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
Taylor, J. P. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg074 · Cited by 426
Eukaryotic Proteasomes Cannot Digest Polyglutamine Sequences and Release Them during Degradation of Polyglutamine-Containing Proteins
Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N., & Goldberg, A. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00151-0 · Cited by 424
Hassles with Taking Out the Garbage: Aggravating Aggresomes
Garcia‐Mata, R., Gao, Y., & Sztul, E. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.30602.x · Cited by 391
The role of pathogenic DJ‐1 mutations in Parkinson's disease
Abou‐Sleiman, P. M., Healy, D. G., Quinn, N., Lees, A. J., & Wood, N. W. (2003) · Annals of Neurology · doi:10.1002/ana.10675 · Cited by 383
Pathologic and biochemical studies of juvenile parkinsonism linked to chromosome 6q
Mori, H., Kondo, T., Yokochi, M., Matsumine, H., Nakagawa-Hattori, Y., Miyake, T., Suda, K., & Mizuno, Y. (1998) · Neurology · doi:10.1212/wnl.51.3.890 · Cited by 370
Parkin Localizes to the Lewy Bodies of Parkinson Disease and Dementia with Lewy Bodies
Schlossmacher, M. G., Frosch, M. P., Gai, W. P., Medina, M., Sharma, N., Forno, L., Ochiishi, T., Shimura, H., Sharon, R., Hattori, N., et al. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)61113-3 · Cited by 325
A regulated interaction with the UIM protein Eps15 implicates parkin in EGF receptor trafficking and PI(3)K–Akt signalling
Fallon, L., Bélanger, C. M. L., Corera, A. T., Kontogiannea, M., Regan-Klapisz, E., Moreau, F., Voortman, J., Haber, M., Rouleau, G., Thorarinsdottir, T., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1441 · Cited by 317
Lewy-body formation is an aggresome-related process: a hypothesis
Olanow, C. W., Perl, D. P., DeMartino, G. N., & McNaught, K. S. P. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00827-0 · Cited by 305
Protein Misfolding and Human Disease
Gregersen, N., Bross, P., Vang, S., & Christensen, J. H. (2006) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.7.080505.115737 · Cited by 301
Inefficient degradation of truncated polyglutamine proteins by the proteasome
Holmberg, C. I., Staniszewski, K. E., Mensah, K. N., Matouschek, A., & Morimoto, R. I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600426 · Cited by 289
Familial Parkinson's Disease-associated L166P Mutation Disrupts DJ-1 Protein Folding and Function
Olzmann, J. A., Brown, K., Wilkinson, K. D., Rees, H. D., Huai, Q., Ke, H., Levey, A. I., Li, L., & Chin, L.-S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311017200 · Cited by 267
Self-citation
Disease-Associated Prion Protein Oligomers Inhibit the 26S Proteasome
Kristiansen, M., Deriziotis, P., Dimcheff, D. E., Jackson, G. S., Ovaa, H., Naumann, H., Clarke, A. R., van Leeuwen, F. W. B., Menéndez-Benito, V., Dantuma, N. P., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.001 · Cited by 263
Familial juvenile Parkinsonism.
Carlier, G., & Jm, D. (1979) · PubMed · Cited by 261
Familial juvenile parkinsonism: Clinical and pathologic study in a family
Takahashi, H., Ohama, E., Suzuki, S., Horikawa, Y., Ishikawa, A., Morita, T., Tsuji, S., & Ikuta, F. (1994) · Neurology · doi:10.1212/wnl.44.3_part_1.437 · Cited by 258
Accumulation of the Authentic Parkin Substrate Aminoacyl-tRNA Synthetase Cofactor, p38/JTV-1, Leads to Catecholaminergic Cell Death
Ko, H. S., von Coelln, R., Sriram, S. R., Kim, S. W., Chung, K. K. K., Pletnikova, O., Troncoso, J., Johnson, B., Saffary, R., Goh, E. L., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2172-05.2005 · Cited by 247
Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress
Moore, D. J., Zhang, L., Troncoso, J., Lee, M. K., Hattori, N., Mizuno, Y., Dawson, T. M., & Dawson, V. L. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi007 · Cited by 245
L166P Mutant DJ-1, Causative for Recessive Parkinson's Disease, Is Degraded through the Ubiquitin-Proteasome System
Miller, D. W., Ahmad, R., Hague, S., Baptista, M. J., Canet-Aviles, R., McLendon, C., Carter, D. M., Zhu, P.-P., Stadler, J., Chandran, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304272200 · Cited by 236
Cytoplasmic dynein/dynactin mediates the assembly of aggresomes
Johnston, J. A., Illing, M. E., & Kopito, R. R. (2002) · Cell Motility · doi:10.1002/cm.10057 · Cited by 226
Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin–protein ligase with monoubiquitylation capacity
Hampe, C., Ardila-Osorio, H., Fournier, M., Brice, A., & Corti, O. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl131 · Cited by 226
Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
Hook, S. S., Orian, A., Cowley, S. M., & Eisenman, R. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172511699 · Cited by 224
A missense mutation (L166P) in DJ‐1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo‐oligomerization
Moore, D. J., Zhang, L., Dawson, T. M., & Dawson, V. L. (2003) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2003.02265.x · Cited by 222
Induction of murine NAD(P)H:quinone oxidoreductase by 2,3,7,8-tetrachlorodibenzo-p-dioxin requires the CNC (cap n collar) basic leucine zipper transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2): cross-interaction between AhR (aryl hydrocarbon receptor) and Nrf2 signal transduction
MA, Q., KINNEER, K., BI, Y., CHAN, J. Y., & KAN, Y. W. (2004) · Biochemical Journal · doi:10.1042/bj20031123 · Cited by 219
An autopsy case of autosomal-recessive juvenile parkinsonism with a homozygous exon 4 deletion in theparkin gene
Hayashi, S., Wakabayashi, K., Ishikawa, A., Nagai, H., Saito, M., Maruyama, M., Takahashi, T., Ozawa, T., Tsuji, S., & Takahashi, H. (2000) · Movement Disorders · doi:10.1002/1531-8257(200009)15:5<884::aid-mds1019>3.0.co;2-8 · Cited by 212
Diverse Effects of Pathogenic Mutations of Parkin That Catalyze Multiple Monoubiquitylation in Vitro
Matsuda, N., Kitami, T., Suzuki, T., Mizuno, Y., Hattori, N., & Tanaka, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510393200 · Cited by 167
Regulation of Synaptophysin Degradation by Mammalian Homologues of Seven in Absentia
Wheeler, T. C., Chin, L.-S., Li, Y., Roudabush, F. L., & Li, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107857200 · Cited by 167
Self-citation
Pathogenetic mechanisms of parkin in Parkinson's disease
Hattori, N., & Mizuno, Y. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16901-8 · Cited by 162
Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress
Li, H. M., Niki, T., Taira, T., Iguchi-Ariga, S. M. M., & Ariga, H. (2005) · Free Radical Research · doi:10.1080/10715760500260348 · Cited by 160
Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function
Periquet, M., Corti, O., Jacquier, S., & Brice, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03442.x · Cited by 160
Novel Monoclonal Antibodies Demonstrate Biochemical Variation of Brain Parkin with Age
Pawlyk, A. C., Giasson, B. I., Sampathu, D. M., Perez, F. A., Lim, K. L., Dawson, V. L., Dawson, T. M., Palmiter, R. D., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306889200 · Cited by 151
Self-citation
Parkin-mediated lysine 63-linked polyubiquitination: A link to protein inclusions formation in Parkinson's and other conformational diseases?
Lim, K., Dawson, V. L., & Dawson, T. M. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.07.023 · Cited by 145
Parkin Accumulation in Aggresomes Due to Proteasome Impairment
Junn, E., Lee, S. S., Suhr, U. T., & Mouradian, M. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203159200 · Cited by 144
Spongiform Neurodegeneration-associated E3 Ligase Mahogunin Ubiquitylates TSG101 and Regulates Endosomal Trafficking
Kim, B. Y., Olzmann, J. A., Barsh, G. S., Chin, L., & Li, L. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0787 · Cited by 142
Self-citation
How does parkin ligate ubiquitin to Parkinson's disease? First in Molecular Medicine Review Series
Kahle, P. J., & Haass, C. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400188 · Cited by 133
α-Synuclein and Parkin Contribute to the Assembly of Ubiquitin Lysine 63-linked Multiubiquitin Chains
Doss-Pepe, E., Chen, L., & Madura, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413591200 · Cited by 131
Staring, a Novel E3 Ubiquitin-Protein Ligase That Targets Syntaxin 1 for Degradation
Chin, L., Vavalle, J. P., & Li, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203300200 · Cited by 123
Self-citation
Inhibition of Proteasomal Activity Causes Inclusion Formation in Neuronal and Non-Neuronal Cells Overexpressing Parkin
Ardley, H. C., Scott, G. B., Rose, S. A., Tan, N. G. S., Markham, A. F., & Robinson, P. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-02-0078 · Cited by 121
Identification of Far Upstream Element-binding Protein-1 as an Authentic Parkin Substrate
Ko, H. S., Kim, S. W., Sriram, S. R., Dawson, V. L., & Dawson, T. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600041200 · Cited by 107
SNIP, a Novel SNAP-25-interacting Protein Implicated in Regulated Exocytosis
Chin, L., Nugent, R. D., Raynor, M., Vavalle, J. P., & Li, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1191 · Cited by 105
Self-citation
Human thiopurine S -methyltransferase pharmacogenetics: Variant allozyme misfolding and aggresome formation
Wang, L., Nguyen, T. V., McLaughlin, R. W., Sikkink, L. A., Ramírez-Alvarado, M., & Weinshilboum, R. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502352102 · Cited by 102
Differential Effects of Parkinson's Disease-associated Mutations on Stability and Folding of DJ-1
Görner, K., Holtorf, E., Odoy, S., Nuscher, B., Yamamoto, A., Regula, J. T., Beyer, K., Haass, C., & Kahle, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309204200 · Cited by 87
Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival
Muqit, M. M. K., Davidson, S. M., Smith, M. D. P., MacCormac, L. P., Kahns, S., Jensen, P. H., Wood, N. W., & Latchman, D. S. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddh012 · Cited by 82
Parkin is recruited to the centrosome in response to inhibition of proteasomes
Zhao, J., Ren, Y., Jiang, Q., & Feng, J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00700 · Cited by 74
Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity
Perez, F. A., Curtis, W., & Palmiter, R. D. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-71 · Cited by 68
Self-citation
Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brain
Baulac, S., LaVoie, M. J., Strahle, J. M., Schlossmacher, M. G., & Xia, W. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.06.014 · Cited by 66
Induction of metallothionein I by phenolic antioxidants requires metal-activated transcription factor 1 (MTF-1) and zinc
Bi, Y., Palmiter, R. D., WOOD, K. M., & Ma, Q. (2004) · Biochemical Journal · doi:10.1042/bj20031677 · Cited by 50
Self-citation
Selective enrichment of DJ‐1 protein in primate striatal neuronal processes: Implications for Parkinson's disease
Olzmann, J. A., Glausier, J. R., Muly, E. C., Rees, H. D., Levey, A. I., Li, L., & Chin, L. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.21191 · Cited by 49
Self-citation
A method to identify p62’s UBA domain interacting proteins
Pridgeon, J. W., Geetha, T., & Wooten, M. W. (2003) · Biological Procedures Online · doi:10.1251/bpo66 · Cited by 24

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438
A Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Dikic, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,239
The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Kwon, Y. T., & Ciechanover, A. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.09.002 · Cited by 817

See all 339

Authors: Olzmann, J. A., Li, L., Chudaev, M. V., Chen, J., Perez, F. A., Palmiter, R. D., & Chin, L.-S.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2007-09-10
Volume: 178
Issue: 6
Pages: 1025-1038
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200611128
OpenAlex: W2115620208
Cited by: 339
References: 78
FWCI: 15.77
Type: journal article
Language: en
Open access: bronze

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.

Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources