Cited by 323Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysCalcium signaling and nucleotide metabolism

The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.

PLIC proteins or ubiquilins regulate autophagy‐dependent cell survival during nutrient starvation

Open access

N'Diaye, Elsa‐Noah, Kajihara, Kimberly K, Hsieh, Ivy, Morisaki, Hiroshi, Debnath, Jayanta, Brown, Eric J·2009·The EMBO Reports

DOI 10.1038/embor.2008.238PMC PMC2637314

Open this paper in CoChat — free account

Abstract

Ubiquilins (UBQLNs) are adaptor proteins thought to deliver ubiquitinated substrates to proteasomes. Here, we show a role for UBQLN in autophagy: enforced expression of UBQLN protects cells from starvation-induced death, whereas depletion of UBQLN renders cells more susceptible. The UBQLN protective effect requires the autophagy-related genes ATG5 and ATG7, two essential components of autophagy. The ubiquitin-associated domain of UBQLN mediates both its association with autophagosomes and its protective effect against starvation. Depletion of UBQLN delays the delivery of autophagosomes to lysosomes. This study identifies a new role for UBQLN in regulating the maturation of autophagy, expanding the involvement of ubiquitin-related proteins in this process.

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 · 10.1038/embor.2008.238

Cites

36 of 36 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.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Autophagy as a Regulated Pathway of Cellular Degradation
Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979

Show all 36 references

Sorted by citations

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Combination of ERK and autophagy inhibition as a treatment approach for pancreatic cancer
Bryant, K. L., Stalnecker, C. A., Zeitouni, D., Klomp, J. E., Peng, S., Tikunov, A. P., Gunda, V., Pierobon, M., Waters, A. M., George, S. D., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0368-8 · Cited by 692
Autophagy mediates degradation of nuclear lamina
Dou, Z., Xu, C., Donahue, G., Shimi, T., Pan, J.-A., Zhu, J., Ivanov, A., Capell, B. C., Drake, A. M., Shah, P. P., et al. (2015) · Nature · doi:10.1038/nature15548 · Cited by 655
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
Kirkin, V., & Rogov, V. V. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.005 · Cited by 536
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 512
The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 499
Autophagic cell death restricts chromosomal instability during replicative crisis
Nassour, J., Radford, R., Correia, A., Fusté, J. M., Schoell, B., Jauch, A., Shaw, R. J., & Karlseder, J. (2019) · Nature · doi:10.1038/s41586-019-0885-0 · Cited by 429
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395
Copper is an essential regulator of the autophagic kinases ULK1/2 to drive lung adenocarcinoma
Tsang, T., Posimo, J. M., Gudiel, A. A., Cicchini, M., Feldser, D. M., & Brady, D. C. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0481-4 · Cited by 373
TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets
Scotter, E. L., Chen, H.-J., & Shaw, C. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0338-x · Cited by 382
Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions
Dao, T. P., Kolaitis, R., Kim, H. J., O’Donovan, K., Martyniak, B., Colicino, E. G., Hehnly, H., Taylor, J. P., & Castañeda, C. A. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.004 · Cited by 341
Hepatic stellate cell autophagy inhibits extracellular vesicle release to attenuate liver fibrosis
Gao, J., Wei, B., de Assuncao, T. M., Liu, Z., Hu, X., Ibrahim, S., Cooper, S. A., Cao, S., Shah, V. H., & Kostallari, E. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.04.044 · Cited by 288
A comprehensive glossary of autophagy-related molecules and processes (2ndedition)
Klionsky, D. J., Baehrecke, E. H., Brumell, J. H., Chu, C. T., Codogno, P., Cuervo, A. M., Debnath, J., Deretic, V. P., Elazar, Z., Eskelinen, E., et al. (2011) · Autophagy · doi:10.4161/auto.7.11.17661 · Cited by 298
Self-citation
ZKSCAN3 Is a Master Transcriptional Repressor of Autophagy
Chauhan, S., Goodwin, J. G., Chauhan, S., Manyam, G., Wang, J., Kamat, A. M., & Boyd, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.024 · Cited by 266
Exploiting cancer cell vulnerabilities to develop a combination therapy for ras-driven tumors
De Raedt, T., Walton, Z., Yecies, J. L., Li, D., Chen, Y., Malone, C. F., Maertens, O., Jeong, S. M., Bronson, R. T., Lebleu, V., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.014 · Cited by 258
Autophagy Receptors and Neurodegenerative Diseases
Deng, Z., Purtell, K., Lachance, V., Wold, M. S., Chen, S., & Yue, Z. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.01.001 · Cited by 243
MAPK1/3 kinase-dependent ULK1 degradation attenuates mitophagy and promotes breast cancer bone metastasis
Deng, R., Zhang, H., Huang, J.-H., Cai, R., Wang, Y., Chen, Y., Hu, B., Ye, Z.-P., Li, Z., Mai, J., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1850609 · Cited by 234
Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225
Protein aggregation and degradation mechanisms in neurodegenerative diseases.
Takalo, M., Salminen, A., Soininen, H. S., Hiltunen, M. O., & Haapasalo, A. (2013) · Europe PMC (PubMed Central) · Cited by 220
Dysregulated molecular pathways in amyotrophic lateral sclerosis–frontotemporal dementia spectrum disorder
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 229
Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates
Park, H., Kang, J., & Lee, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093369 · Cited by 216
Impairment of the autophagy–lysosomal pathway in Alzheimer's diseases: Pathogenic mechanisms and therapeutic potential
Zhang, W., Xu, C., Sun, J., Shen, H., Wang, J., & Yang, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.008 · Cited by 219
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
“UBQLN2 can also act as an autophagy receptor by directly interacting with LC3 in autophagosomes [219,220].”
Background
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 203
Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
Brettschneider, J., Deerlin, V. M. V., Robinson, J. L., Kwong, L. K., Lee, E. B., Ali, Y., Safren, N., Monteiro, M. J., Toledo, J. B., Elman, L. B., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0970-z · Cited by 187
A comprehensive glossary of autophagy-related molecules and processes
Klionsky, D. J., Codogno, P., Cuervo, A. M., Deretic, V. P., Elazar, Z., Fueyo-Margareto, J., Gewirtz, D. A., Kroemer, G., Levine, B., Mizushima, N., et al. (2010) · Autophagy · doi:10.4161/auto.6.4.12244 · Cited by 185
iLIR database: A web resource for LIR motif-containing proteins in eukaryotes
Jacomin, A., Samavedam, S., Promponas, V. J., & Nezis, I. P. (2016) · Autophagy · doi:10.1080/15548627.2016.1207016 · Cited by 183
Combination Therapies with CDK4/6 Inhibitors to Treat KRAS- Mutant Pancreatic Cancer
Goodwin, C. M., Waters, A. M., Klomp, J. E., Javaid, S., Bryant, K. L., Stalnecker, C. A., Drizyte-Miller, K., Papke, B., Yang, R., Amparo, A. M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-0391 · Cited by 168
The ubiquitin–proteasome system in kidney physiology and disease
Meyer‐Schwesinger, C. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0148-1 · Cited by 164
FOXO3 directly regulates an autophagy network to functionally regulate proteostasis in adult neural stem cells
Audesse, A. J., Dhakal, S., Hassell, L.-A., Gardell, Z., Nemtsova, Y., & Webb, A. E. (2019) · PLOS Genetics · doi:10.1371/journal.pgen.1008097 · Cited by 155
Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation
Su, V., & Lau, A. F. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0048-9 · Cited by 147
FoxO Function Is Essential for Maintenance of Autophagic Flux and Neuronal Morphogenesis in Adult Neurogenesis
Schäffner, I., Minakaki, G., Khan, M. A., Balta, E.-A., Schlötzer-Schrehardt, U., Schwarz, T. J., Beckervordersandforth, R., Winner, B., Webb, A. E., DePinho, R. A., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.08.017 · Cited by 145
“To further validate impaired autophagic flux and the identity of accumulated autophagy-related structures in FoxO cKO cells, we employed a tandem monomeric mCherry-GFP-tagged LC3 reporter (mCherry/GFP/LC3) (N’Diaye et al., 2009; Pankiv et al., 2007), which takes advantage of the differential pH sensitivity of the mChe…”
p27 controls Ragulator and mTOR activity in amino acid-deprived cells to regulate the autophagy–lysosomal pathway and coordinate cell cycle and cell growth
Nowosad, A., Jeannot, P., Callot, C., Creff, J., Perchey, R. T., Joffre, C., Codogno, P., Manenti, S., & Besson, A. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0554-4 · Cited by 144
Mitochondrial-derived vesicles compensate for loss of LC3-mediated mitophagy
Towers, C. G., Wodetzki, D., Thorburn, J., Smith, K. R., Caino, M. C., & Thorburn, A. M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.06.003 · Cited by 143
Glucagon-Like Peptide 1 Protects Pancreatic β-Cells From Death by Increasing Autophagic Flux and Restoring Lysosomal Function
Zummo, F. P., Cullen, K. S., Honkanen‐Scott, M., Shaw, J., Lovat, P. E., & Arden, C. (2017) · Diabetes · doi:10.2337/db16-1009 · Cited by 140
Ubiquilin Modifies TDP-43 Toxicity in a Drosophila Model of Amyotrophic Lateral Sclerosis (ALS)
Hanson, K. A., Kim, S. H., Wassarman, D. A., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.078527 · Cited by 133
Genome‐wide siRNA screen reveals amino acid starvation‐induced autophagy requires SCOC and WAC
McKnight, N. C., Jefferies, H. B. J., Alemu, E. A., Saunders, R. E., Howell, M. T., Johansen, T., & Tooze, S. A. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.36 · Cited by 127
Interleukin-6 Reduces β-Cell Oxidative Stress by Linking Autophagy With the Antioxidant Response
Marasco, M. R., Conteh, A. M., Reissaus, C. A., Cupit, J. E., Appleman, E. M., Mirmira, R. G., & Linnemann, A. K. (2018) · Diabetes · doi:10.2337/db17-1280 · Cited by 129
Autophagy: links with the proteasome
Lamark, T., & Johansen, T. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.002 · Cited by 124
Mechanisms of neuronal homeostasis: Autophagy in the axon
Maday, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.047 · Cited by 130
The Roles of Ubiquitin-Binding Protein Shuttles in the Degradative Fate of Ubiquitinated Proteins in the Ubiquitin-Proteasome System and Autophagy
Zientara‐Rytter, K., & Subramani, S. E. (2019) · Cells · doi:10.3390/cells8010040 · Cited by 124
Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification
Şentürk, M., Lin, G., Zuo, Z., Mao, D., Watson, E., Mikos, A. G., & Bellen, H. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0281-x · Cited by 124
Vitamin D receptor regulates autophagy in the normal mammary gland and in luminal breast cancer cells
Tavera-Mendoza, L. E., Westerling, T., Libby, E., Marusyk, A., Cato, L., Cassani, R., Cameron, L., Ficarro, S. B., Marto, J. A., Klawitter, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615015114 · Cited by 124
p27 controls autophagic vesicle trafficking in glucose-deprived cells via the regulation of ATAT1-mediated microtubule acetylation
Nowosad, A., Creff, J., Jeannot, P., Culerrier, R. M., Codogno, P., Manenti, S., Nguyen, L., & Besson, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03759-9 · Cited by 128
Key role of UBQLN2 in pathogenesis of amyotrophic lateral sclerosis and frontotemporal dementia
Renaud, L., Picher‐Martel, V., Codron, P., & Julien, J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0758-7 · Cited by 119
Atg5-Independent Sequestration of Ubiquitinated Mycobacteria
Collins, C. A., Mazière, A. M. G. L. D., van Dijk, S., Carlsson, F., Klumperman, J., & Brown, E. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000430 · Cited by 124
Self-citation
Regulation of liquid–liquid phase separation with focus on post-translational modifications
Luo, Y.-Y., Wu, J., & Li, Y. (2021) · Chemical Communications · doi:10.1039/d1cc05266g · Cited by 121
Autophagy is essential for oligodendrocyte differentiation, survival, and proper myelination
Bankston, A. N., Forston, M. D., Howard, R. M., Andres, K. R., Smith, A. E., Ohri, S. S., Bates, M. L., Bunge, M. B., & Whittemore, S. R. (2019) · Glia · doi:10.1002/glia.23646 · Cited by 112
AMPK Inhibits ULK1-Dependent Autophagosome Formation and Lysosomal Acidification via Distinct Mechanisms
Nwadike, C., Williamson, L. E., Gallagher, L. E., Guan, J.-L., & Chan, E. Y. W. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00023-18 · Cited by 110
Hypoxia promotes noncanonical autophagy in nucleus pulposus cells independent of MTOR and HIF1A signaling
Choi, H., Merceron, C., Mangiavini, L., Seifert, E. L., Schipani, E., Shapiro, I. M., & Risbud, M. V. (2016) · Autophagy · doi:10.1080/15548627.2016.1192753 · Cited by 111
Autophagy as a common pathway in amyotrophic lateral sclerosis
Nguyen, D. K. H., Thombre, R., & Wang, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.006 · Cited by 118
The IAP family member BRUCE regulates autophagosome–lysosome fusion
Ebner, P., Poetsch, I., Deszcz, L., Hoffmann, T., Zuber, J. A., & Ikeda, F. (2018) · Nature Communications · doi:10.1038/s41467-018-02823-x · Cited by 104
Phosphatidylinositol-5-Phosphate 4-Kinases Regulate Cellular Lipid Metabolism By Facilitating Autophagy
Lundquist, M. R., Goncalves, M. D., Loughran, R. M., Possik, E., Vijayaraghavan, T., Yang, A., Pauli, C., Ravi, A., Verma, A., Yang, Z., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.037 · Cited by 111
HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons
Guedes-Dias, P., de Proença, J., Soares, T. R., Leitão-Rocha, A., Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.012 · Cited by 106
Interplay Between the Autophagy-Lysosomal Pathway and the Ubiquitin-Proteasome System: A Target for Therapeutic Development in Alzheimer’s Disease
Bustamante, H. A., González, A., Cerda‐Troncoso, C., Shaughnessy, R., Carola Otth, L., Soza, A., & Burgos, P. V. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00126 · Cited by 102
Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbances
Vollrath, J. T., Sechi, A. S., Dreser, A., Katona, I., Wiemuth, D., Vervoorts, J., Dohmen, M., Chandrasekar, A., Prause, J. U., Brauers, E., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.243 · Cited by 104
Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis
Sundaramoorthy, V., Walker, A. K., Tan, V. X., Fifita, J. A., McCann, E. P., Williams, K. L., Blair, I. P., Guillemin, G. J., Farg, M. A., & Atkin, J. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv126 · Cited by 103
Crosstalk Between Macroautophagy and Chaperone-Mediated Autophagy: Implications for the Treatment of Neurological Diseases
Wu, H., Chen, S., Al-Baadani, A., Xu, J., Wu, Q., Pan, K., Zhang, J., & Hong, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8933-0 · Cited by 103
Paradoxical resistance of multiple myeloma to proteasome inhibitors by decreased levels of 19S proteasomal subunits
Acosta‐Alvear, D., Cho, M. Y., Wild, T., Buchholz, T. J., Lerner, A. G., Šimáková, O., Hahn, J., Korde, N., Landgren, O., Marić, I., et al. (2015) · eLife · doi:10.7554/elife.08153 · Cited by 94
Autophagy receptor defects and ALS-FTLD
Majcher, V., Goode, A., James, V. H., & Layfield, R. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.002 · Cited by 101
ALS/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function
Wu, J. J., Cai, A., Greenslade, J. E., Higgins, N. R., Fan, C., Le, N. T. T., Tatman, M., Whiteley, A. M., Prado, M. A., Dieriks, B. V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917371117 · Cited by 86
Regulation of GPCR signal networks via membrane trafficking
Jean‐Alphonse, F., & Hanyaloglu, A. C. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.07.010 · Cited by 95
Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein
Stieren, E. S., Ayadi, A. E., Xiao, Y., Siller, E., Landsverk, M., Oberhauser, A. F., Barral, J. M., & Boehning, D. F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243147 · Cited by 91
Targeting SQSTM1/p62 Induces Cargo Loading Failure and Converts Autophagy to Apoptosis via NBK/Bik
Chen, S., Zhou, L., Zhang, Y., Leng, Y., Pei, X.-Y., Lin, H., Jones, R., Orlowski, R. Z., Dai, Y., & Grant, S. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01383-13 · Cited by 92
Motor neuron disease, TDP-43 pathology, and memory deficits in mice expressing ALS–FTD-linked UBQLN2 mutations
Le, N. T. T., Chang, L., Kovlyagina, I., Georgiou, P., Safren, N., Braunstein, K. E., Kvarta, M. D., Dyke, A. M. V., LeGates, T. A., Philips, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608432113 · Cited by 89
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome
Chen, X., Randles, L., Shi, K., Tarasov, S. G., Aihara, H., & Walters, K. J. (2016) · Structure · doi:10.1016/j.str.2016.05.018 · Cited by 84
Autophagy-induced senescence is regulated by p38α signaling
Slobodnyuk, K., Radic, N., Ivanova, S., Lladó, A., Trempolec, N., Antonio Zorzano, A., & Nebreda, Á. R. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1607-0 · Cited by 90
Eps15: a multifunctional adaptor protein regulating intracellular trafficking
Henegouwen, P. M. P. V. B. E. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-24 · Cited by 88
CYLD is a causative gene for frontotemporal dementia – amyotrophic lateral sclerosis
Dobson‐Stone, C., Hallupp, M., Shahheydari, H., Ragagnin, A., Chatterton, Z., Carew‐Jones, F., Shepherd, C. E., Stefen, H., Parić, E., Fath, T., et al. (2020) · Brain · doi:10.1093/brain/awaa039 · Cited by 86
Hederagenin potentiated cisplatin- and paclitaxel-mediated cytotoxicity by impairing autophagy in lung cancer cells
Wang, K., Liu, X., Liu, Q., Ho, I. H. T., Wei, X., Yin, T., Zhan, Y., Zhang, W., Zhang, W., Chen, B., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02880-5 · Cited by 88
HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis
Watanabe, Y., Tsujimura, A., Taguchi, K., & Tanaka, M. (2016) · Autophagy · doi:10.1080/15548627.2016.1248018 · Cited by 87
The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
Metcalf, D. J., & Isaacs, A. M. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381469 · Cited by 90
Ubiquilin 1 Promotes IFN-γ-Induced Xenophagy of Mycobacterium tuberculosis
Sakowski, E. T., Köster, S., Portal‐Celhay, C., Park, H. S., Shrestha, E., Hetzenecker, S. E. G., Maurer, K., Cadwell, K., & Philips, J. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005076 · Cited by 85
Propranolol sensitizes prostate cancer cells to glucose metabolism inhibition and prevents cancer progression
Brohée, L., Peulen, O., Nusgens, B., Castronovo, V., Thiry, M., Colige, A., & Deroanne, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-25340-9 · Cited by 81
Plac8 Links Oncogenic Mutations to Regulation of Autophagy and Is Critical to Pancreatic Cancer Progression
Kinsey, C. G., Balakrishnan, V., O’Dell, M. R., Huang, J. L., Newman, L. A., Whitney‐Miller, C. L., Hezel, A. F., & Land, H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.061 · Cited by 81
Lipin-1 regulates cancer cell phenotype and is a potential target to potentiate rapamycin treatment
Brohée, L., Demine, S., Willems, J., Arnould, T., Colige, A., & Deroanne, C. (2015) · Oncotarget · doi:10.18632/oncotarget.3595 · Cited by 80
Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion
Lindqvist, L., Frank, D. O., McArthur, K., Dite, T. A., Lazarou, M., Oakhill, J. S., Kile, B. T., & Vaux, D. L. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0017-z · Cited by 82
Causative Genes in Amyotrophic Lateral Sclerosis and Protein Degradation Pathways: a Link to Neurodegeneration
Maurel, C., Dangoumau, A., Marouillat, S., Brulard, C., Chami, A. A., Hergesheimer, R. C., Corcia, P., Blasco, H., Andres, C. R., & Vourc’h, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0856-0 · Cited by 80
Impairment of Lysosome Function and Autophagy in Rare Neurodegenerative Diseases
Darios, F. D., & Stévanin, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.033 · Cited by 78
Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery
Lee, D. Y., Arnott, D. P., & Brown, E. J. (2013) · EMBO Reports · doi:10.1038/embor.2013.22 · Cited by 78
Self-citation
RAD51AP1 Is an Essential Mediator of Alternative Lengthening of Telomeres
González, J. B., García-Expósito, L., Hoang, S. M., Lynskey, M. L., Roncaioli, J. L., Ghosh, A., Wallace, C. T., de Vitis, M., Modesti, M., Bernstein, K. A., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.043 · Cited by 77
Defective Proteasome Delivery of Polyubiquitinated Proteins by Ubiquilin-2 Proteins Containing ALS Mutations
Chang, L., & Monteiro, M. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130162 · Cited by 76
Selective Autophagy Receptors in Neuronal Health and Disease
Conway, O., Akpinar, H. A., Rogov, V. V., & Kirkin, V. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.013 · Cited by 75
TBC1D20 mediates autophagy as a key regulator of autophagosome maturation
Sidjanin, D. J., Park, A. K., Ronchetti, A., Martins, J., & Jackson, W. T. (2016) · Autophagy · doi:10.1080/15548627.2016.1199300 · Cited by 79
A nonapoptotic role for CASP2/caspase 2
Tiwari, M., Sharma, L. K., Vanegas, D., Callaway, D. A., Bai, Y., Lechleiter, J. D., & Herman, B. A. (2014) · Autophagy · doi:10.4161/auto.28528 · Cited by 78
Pathogenic Ubqln2 gains toxic properties to induce neuron death
Wu, Q., Liu, M., Huang, C., Liu, X., Huang, B., Li, N., Zhou, H., & Xia, X. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1367-y · Cited by 73
Leelamine Mediates Cancer Cell Death through Inhibition of Intracellular Cholesterol Transport
Kuzu, O. F., Gowda, R., Sharma, A. K., & Robertson, G. P. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0868 · Cited by 80
Ubiquitin receptors and protein quality control
Wang, X., & Terpstra, E. J. M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.09.012 · Cited by 75
Impaired protein degradation in FTLD and related disorders
Götzl, J. K., Lang, C. M., Haass, C., & Capell, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.008 · Cited by 74
Modulating cancer cell survival by targeting intracellular cholesterol transport
Kuzu, O. F., Gowda, R., Noory, M. A., & Robertson, G. P. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.200 · Cited by 73
The ubiquilin gene family: evolutionary patterns and functional insights
Marı́n, I. (2014) · BMC Evolutionary Biology · doi:10.1186/1471-2148-14-63 · Cited by 71
Alzheimer's Disease‐Associated Ubiquilin‐1 Regulates Presenilin‐1 Accumulation and Aggresome Formation
Viswanathan, J., Haapasalo, A., Böttcher, C., Miettinen, R. A., Kurkinen, K. M. A., Lu, A., Thomas, A., Maynard, C. J., Romano, D., Hyman, B. T., et al. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01149.x · Cited by 71
ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1
Soo, K. Y., Sultana, J. M., King, A. E., Atkinson, R., Warraich, S. T., Sundaramoorthy, V., Blair, I. P., Farg, M. A., & Atkin, J. D. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.30 · Cited by 69
Activated MLKL attenuates autophagy following its translocation to intracellular membranes
Frank, D. O., Vaux, D. L., Murphy, J. M., Vince, J. E., & Lindqvist, L. (2019) · Journal of Cell Science · doi:10.1242/jcs.220996 · Cited by 72
Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like protein, BCL2L10/BCLb, are regulated by Ubiquilin1
Beverly, L. J., Lockwood, W. W., Shah, P. P., Erdjument‐Bromage, H., & VARMUS, H. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119167109 · Cited by 73
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69
Novel UBQLN2 mutations linked to amyotrophic lateral sclerosis and atypical hereditary spastic paraplegia phenotype through defective HSP70-mediated proteolysis
Teyssou, E., Chartier, L., Amador, M. D. M., Lam, R., Lautrette, G., Nicol, M., Machat, S., da Barroca, S., Moigneu, C., Mairey, M., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.06.018 · Cited by 67
Protective autophagy decreases osimertinib cytotoxicity through regulation of stem cell-like properties in lung cancer
Li, L., Wang, Y., Jiao, L., Lin, C., Lu, C., Zhang, K., Hu, C., Ye, J., Zhang, D., Wu, H., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.03.027 · Cited by 67
Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: Characterization of inhibition by nucleic acids and 4-aminoquinolines
Cassel, J. A., & Reitz, A. B. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.020 · Cited by 63
RNA‐binding proteins in neurodegenerative disease: TDP‐43 and beyond
Hanson, K. A., Kim, S. H., & Tibbetts, R. S. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.111 · Cited by 67

Authors: N'Diaye, E., Kajihara, K. K., Hsieh, I., Morisaki, H., Debnath, J., & Brown, E. J.
Affiliations: Genentech (US)
ORCID: Kajihara, Kimberly K
Morisaki, Hiroshi
Debnath, Jayanta
Brown, Eric J
Venue: The EMBO Reports
Publisher: Springer Science and Business Media LLC
Published: 2009-01-16
Volume: 10
Issue: 2
Pages: 173-179
ISSN: 1469-221X (ISSN-L)
1469-3178
DOI: 10.1038/embor.2008.238
PMC: PMC2637314
OpenAlex: W2144022982
Cited by: 323
References: 36
Citations by year: 2026: 11 · 2025: 14 · 2024: 16 · 2023: 25 · 2022: 20 · 2021: 22 · 2020: 39 · 2019: 25 · 2018: 30 · 2017: 31 · 2016: 22 · 2015: 18 · 2014: 12 · 2013: 12 · 2012: 5
FWCI: 5.85
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: EMBO Reports (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Washington University in St. Louis
National Institutes of Health
University of California, San Francisco
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: ubiquilin, autophagy, nutrient deprivation, ATG5, ATG7, ubiquitin-associated domain, autophagosome maturation, autophagosome-lysosome fusion, cell survival
MeSH terms: Autophagy-Related Proteins, Autophagy-Related Protein 5, Autophagy-Related Protein 7, Animals, Autophagy, Carrier Proteins, Culture Media, HeLa Cells, Humans, Microtubule-Associated Proteins, Phagosomes, Recombinant Fusion Proteins, Ubiquitins, Microscopy, Immunoelectron, Protein Structure, Tertiary, Cell Cycle Proteins, Protein Interaction Mapping, Adaptor Proteins, Vesicular Transport, RNA Interference, RNA, Small Interfering, Ubiquitin-Activating Enzymes, Adaptor Proteins, Signal Transducing, Mice

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

PLIC proteins or ubiquilins regulate autophagy‐dependent cell survival during nutrient starvation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks