Role of p62/SQSTM1 in liver physiology and pathogenesis
Open accessAbstract
p62/sequestosome-1/A170/ZIP (hereafter referred to as p62) is a scaffold protein that has multiple functions, such as signal transduction, cell proliferation, cell survival, cell death, inflammation, tumourigenesis and oxidative stress response. While p62 is an autophagy substrate and is degraded by autophagy, p62 serves as an autophagy receptor for selective autophagic clearance of protein aggregates and organelles. Moreover, p62 functions as a signalling hub for various signalling pathways, including NF-κB, Nrf2 and mTOR. In this review, we discuss the pathophysiological role of p62 in the liver, including formation of hepatic inclusion bodies, cholestasis, obesity, insulin resistance, liver cell death and tumourigenesis.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
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?
SQSTM1 mutations affect muscle, bone, and liver.
“SQSTM1 mutations affect muscle, bone, and liver [125,367,368]”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [368]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509 · see citing works
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 · see citing works
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · see citing works
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941 · see citing works
A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359 · see citing works
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 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
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 · see citing works
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 · see citing works
Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,422 · see citing works
NF-κB functions as a tumour promoter in inflammation-associated cancer
Pikarsky, E., Porat, R., Stein, I., Abramovitch, R., Amit, S., Kasem, S., Gutkovich-Pyest, E., Urieli-Shoval, S., Galun, E., & Ben-Neriah, Y. (2004) · Nature · doi:10.1038/nature02924 · Cited by 2,295 · see citing works
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 · see citing works
Mammalian autophagy: core molecular machinery and signaling regulation
Yang, Z., & Klionsky, D. J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.014 · Cited by 1,956 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
Autophagy Suppresses Tumorigenesis through Elimination of p62
Mathew, R., Karp, C. M., Beaudoin, B., Vuong, N., Chen, G., Chen, H.-Y., Bray, K., Reddy, A., Bhanot, G., Gélinas, C., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.048 · Cited by 1,721 · see citing works
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works
Termination of autophagy and reformation of lysosomes regulated by mTOR
Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544 · see citing works
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529 · see citing works
Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution
Taguchi, K., Motohashi, H., & Yamamoto, M. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01473.x · Cited by 1,478 · see citing works
Jain, A., Lamark, T., Sjøttem, E., Bowitz Larsen, K., Atesoh Awuh, J., Øvervatn, A., McMahon, M., Hayes, J. D., & Johansen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.118976 · Cited by 1,472 · see citing works
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
Autophagy-deficient mice develop multiple liver tumors
Takamura, A., Komatsu, M., Hara, T., Sakamoto, A., Kishi, C., Waguri, S., Eishi, Y., Hino, O., Tanaka, K., & Mizushima, N. (2011) · Genes & Development · doi:10.1101/gad.2016211 · Cited by 1,342 · cited 2× · see citing works
“Mice with specific deletion of either Atg7 or Atg5 in the liver have spontaneous development of liver adenoma, and high levels of p62 protein have been found in these mouse livers.(52,107) More importantly, Atg7/p62 DKO mice have significantly decreased liver tumourigenesis,(52) which convincingly support the notion t…”
BackgroundJNK1-Mediated Phosphorylation of Bcl-2 Regulates Starvation-Induced Autophagy
Wei, Y., Pattingre, S., Sinha, S., Bassik, M., & Levine, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.001 · Cited by 1,329 · see citing works
NF-κB and STAT3 – key players in liver inflammation and cancer
He, G., & Karin, M. (2010) · Cell Research · doi:10.1038/cr.2010.183 · Cited by 1,197 · see citing works
Maeda, S., Kamata, H., Luo, J., Leffert, H. L., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2005.04.014 · Cited by 1,165 · see citing works
A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates
Kirkin, V., Lamark, T., Sou, Y., Bjørkøy, G., Nunn, J. A. L., Bruun, J., Shvets, E., McEwan, D. G., Clausen, T. H., Wild, P. S., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.020 · Cited by 1,156 · see citing works
Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102 · see citing works
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · see citing works
p62 at the crossroads of autophagy, apoptosis, and cancer
Moscat, J., & Diaz-Meco, M. T. (2009) · Cell · doi:10.1016/j.cell.2009.05.023 · Cited by 1,073 · see citing works
The role of the Atg1/ULK1 complex in autophagy regulation
Mizushima, N. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.004 · Cited by 1,062 · see citing works
Potential therapeutic applications of autophagy
Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 1,004 · see citing works
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works
NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870 · see citing works
Lau, A., Wang, X.-J., Zhao, F. L., Villeneuve, N. F., Wu, T., Jiang, T., Sun, Z., White, E., & Zhang, D. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00248-10 · Cited by 851 · see citing works
Nrf2 enhances resistance of cancer cells to chemotherapeutic drugs, the dark side of Nrf2
Wang, X.-J., Sun, Z., Villeneuve, N. F., Zhang, S., Zhao, F., Li, Y., Chen, W., Yi, X., Zheng, W., Wondrak, G. T., et al. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn095 · Cited by 839 · see citing works
Structural Basis for Sorting Mechanism of p62 in Selective Autophagy
Ichimura, Y., Kumanomidou, T., Sou, Y.-S., Mizushima, T., Ezaki, J., Ueno, T., Kominami, E., Yamane, T., Tanaka, K., & Komatsu, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802182200 · Cited by 803 · see citing works
Ubiquitination and selective autophagy
Shaid, S., Brandts, C. H., Serve, H., & Dikic, I. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.72 · Cited by 800 · see citing works
Narendra, D. P., Kane, L. A., Hauser, D. N., Fearnley, I. M., & Youle, R. J. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 789 · see citing works
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756 · see citing works
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 · see citing works
Seibenhener, M. L., Babu, J. R., Geetha, T., Wong, H. C., Krishna, N. R., & Wooten, M. W. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8055-8068.2004 · Cited by 710 · see citing works
Ding, W.-X., Ni, H.-M., Gao, W., Yoshimori, T., Stolz, D. B., Ron, D., & Yin, X.-M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070188 · Cited by 708 · see citing works
Self-citationMatsumoto, G., Wada, K., Okuno, M., Kurosawa, M., & Nukina, N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.039 · Cited by 694 · see citing works
Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
Blommaart, E. F. C., Luiken, J. J. F. P., Blommaart, P. J. E., van Woerkom, G. M., & Meijer, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2320 · Cited by 686 · see citing works
LAU, A., VILLENEUVE, N., Sun, Z., Wong, P. K., & Zhang, D. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.09.003 · Cited by 645 · see citing works
Selective autophagy: ubiquitin-mediated recognition and beyond
Kraft, C., Peter, M., & Hofmann, K. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-836 · Cited by 639 · see citing works
p62 Is a Common Component of Cytoplasmic Inclusions in Protein Aggregation Diseases
Zatloukal, K., Stumptner, C., Fuchsbichler, A., Heid, H., Schnoelzer, M., Kenner, L., Kleinert, R., Prinz, M., Aguzzi, A., & Denk, H. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64369-6 · Cited by 624 · see citing works
An Emerging Role of mTOR in Lipid Biosynthesis
Laplante, M., & Sabatini, D. M. (2009) · Current Biology · doi:10.1016/j.cub.2009.09.058 · Cited by 614 · see citing works
Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612 · see citing works
Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
Inami, Y., Waguri, S., Sakamoto, A., Kouno, T., Nakada, K., Hino, O., Watanabe, S., Ando, J., Iwadate, M., Yamamoto, M. P., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201102031 · Cited by 602 · see citing works
Deletion of NEMO/IKKγ in Liver Parenchymal Cells Causes Steatohepatitis and Hepatocellular Carcinoma
Luedde, T., Beraza, N., Kotsikoris, V., Loo, G., Nenci, A., Vos, R. D., Roskams, T., Trautwein, C., & Pasparakis, M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.016 · Cited by 596 · see citing works
Jin, Z., Li, Y., Pitti, R. M., Lawrence, D. A., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 588 · see citing works
Ding, W.-X., Ni, H., Li, M., Liao, Y., Chen, X., Stolz, D. B., Dorn, G. W., & Yin, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.119537 · Cited by 586 · see citing works
Self-citationShiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · cited 2× · see citing works
“In addition to the removal of ubiquitinated protein aggregates, p62 also plays an important role in selective removal of mitochondria,66,67 peroxisomes,56 midbody ring structures,68 and bacteria.57,69 When mitochondria are depolarized by uncouplers such as carbonyl cyanide m-chlorophenyl hydrazone (CCCP), the ubiquiti…”
BackgroundThe role of MAPKs in adipocyte differentiation and obesity
Bost, F., Aouadi, M., Caron, L., & Binétruy, B. (2004) · Biochimie · doi:10.1016/j.biochi.2004.10.018 · Cited by 571 · see citing works
Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone.
Laurin, N., Brown, J. P., Morissette, J., & Raymond, V. (2002) · The American Journal of Human Genetics · doi:10.1086/340731 · Cited by 563 · see citing works
The Signaling Adaptor p62 Is an Important NF-κB Mediator in Tumorigenesis
Duran, A., Linares, J. F., Galvez, A. S., Wikenheiser, K., Flores, J. M., Diaz-Meco, M. T., & Moscat, J. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.02.001 · Cited by 541 · see citing works
Nguyen, D. M., & El-Serag, H. B. (2010) · Gastroenterology Clinics of North America · doi:10.1016/j.gtc.2009.12.014 · Cited by 531 · see citing works
Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
Kim, P. K., Hailey, D. W., Mullen, R. T., & Lippincott‐Schwartz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810611105 · Cited by 531 · see citing works
Intracellular Signaling Mechanisms of Acetaminophen-Induced Liver Cell Death
Jaeschke, H., & Bajt, M. L. (2005) · Toxicological Sciences · doi:10.1093/toxsci/kfi336 · Cited by 529 · see citing works
Physiological significance of selective degradation of p62 by autophagy
Komatsu, M., & Ichimura, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.017 · Cited by 516 · see citing works
p62 Is a Key Regulator of Nutrient Sensing in the mTORC1 Pathway
Durán, Á., Amanchy, R., Linares, J. F., Joshi, J. P., Abu‐Baker, S., Porollo, A., Hansen, M., Moscat, J., & Díaz-Meco, M. T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.038 · Cited by 502 · see citing works
Bae, S. H., Sung, S. H., Oh, S. Y., Lim, J. M., Lee, S. K., Park, Y. N., Lee, H. E., Kang, D., & Rhee, S. G. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.002 · Cited by 492 · see citing works
Seki, E., Brenner, D. A., & Karin, M. (2012) · Gastroenterology · doi:10.1053/j.gastro.2012.06.004 · Cited by 488 · see citing works
Keap1 degradation by autophagy for the maintenance of redox homeostasis
Taguchi, K., Fujikawa, N., Komatsu, M., Ishii, T., Unno, M., Akaike, T., Motohashi, H., & Yamamoto, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121572109 · Cited by 482 · see citing works
Amino acids and mTORC1: from lysosomes to disease
Efeyan, A., Zoncu, R., & Sabatini, D. M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.007 · Cited by 436 · cited 1× · see citing works
“Growth factors or insulin activates classI-phosphatidylinosital-3 kinase (PI3K) and AKT, which leads to mTOR activation through the tuberous sclerosis complex protein (TSC)-Rheb signalling cascade.(142) Activation of mTOR then shuts down autophagy, which is a cellular catabolic process, by regulating the ULK1-FIP200At…”
BackgroundThe atypical PKC‐interacting protein p62 channels NF‐κB activation by the IL‐1–TRAF6 pathway
Sanz, L., Diaz‐Meco, M. T., Nakano, H., & Moscat, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1576 · Cited by 436 · see citing works
Filimonenko, M., Isakson, P., Finley, K. D., Anderson, M. R., Jeong, H., Melia, T. J., Bartlett, B. J., Myers, K. M., Birkeland, H. C. G., Lamark, T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.007 · Cited by 432 · see citing works
Activation of Autophagy Protects Against Acetaminophen–Induced Hepatotoxicity
Ni, H., Bockus, A. B., Boggess, N., Jaeschke, H., & Ding, W. (2011) · Hepatology · doi:10.1002/hep.24690 · Cited by 429 · see citing works
Self-citationp62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
Itakura, E., & Mizushima, N. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009067 · Cited by 415 · see citing works
The interaction of p62 with RIP links the atypical PKCs to NF‐κB activation
Sanz, L., Sánchez‐Gómez, P., Lallena, M., Díaz-Meco, M. T., & Moscat, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.3044 · Cited by 410 · see citing works
Obesity and hepatocellular carcinoma
Caldwell, S. H., Crespo, D. M., Kang, H. S., & Al‐Osaimi, A. M. S. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.09.021 · Cited by 396 · see citing works
Ding, W., & Yin, X.-M. (2008) · Autophagy · doi:10.4161/auto.5190 · Cited by 383 · see citing works
Self-citationPuissant, A., Robert, G., Fenouille, N., Luciano, F., Cassuto, J., Raynaud, S., & Auberger, P. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3537 · Cited by 375 · see citing works
Young, M. M., Takahashi, Y., Khan, O. A., Park, S., Hori, T., Yun, J. K., Sharma, A. K., Amin, S., Hu, C., Zhang, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309104 · Cited by 372 · see citing works
Iida, K., Itoh, K., Kumagai, Y., Oyasu, R., Hattori, K., Kawai, K., Shimazui, T., Akaza, H., & Yamamoto, M. P. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1906 · Cited by 372 · see citing works
Kwak, M., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · Molecular Medicine · doi:10.1007/bf03401947 · Cited by 357 · see citing works
Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget’s disease.
Hocking, L. J. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.22.2735 · Cited by 350 · see citing works
From Mallory to Mallory–Denk bodies: What, how and why?
Zatloukal, K., French, S. W., Stumptner, C., Strnad, P., Harada, M., Toivola, D. M., Cadrin, M., & Omary, M. B. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.04.024 · Cited by 341 · see citing works
Bost, F., Aouadi, M., Caron, L., Even, P. C., Belmonte, N., Prot, M., Dani, C., Hofman, P. M., Pagès, G., Pouysségur, J., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.2.402 · Cited by 337 · see citing works
Kwak, M.-K., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · PubMed Central · Cited by 330 · see citing works
Clausen, T. H., Lamark, T., Isakson, P., Finley, K. D., Larsen, K. B., Brech, A., Øvervatn, A., Stenmark, H., Bjørkøy, G., Simonsen, A., et al. (2010) · Autophagy · doi:10.4161/auto.6.3.11226 · Cited by 321 · see citing works
Durán, A., Serrano, M., Leitges, M., Flores, J. M., Picard, S., Brown, J. P., Moscat, J., & Diaz-Meco, M. T. (2004) · Developmental Cell · doi:10.1016/s1534-5807(03)00403-9 · Cited by 316 · see citing works
Signal integration and diversification through the p62 scaffold protein
Moscat, J., Díaz-Meco, M. T., & WOOTEN, M. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.12.002 · Cited by 315 · see citing works
Ponpuak, M., Davis, A. S., Roberts, E. A., Delgado, M. A., Dinkins, C., Zhao, Z., Virgin, H. W., Kyei, G. B., Johansen, T., Vergne, I., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.02.009 · Cited by 308 · see citing works
p62/SQSTM1/A170: Physiology and pathology
Komatsu, M., Kageyama, S., & Ichimura, Y. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.07.004 · Cited by 301 · see citing works
Mature-onset obesity and insulin resistance in mice deficient in the signaling adapter p62
Rodriguez, A., Durán, A., Selloum, M., Champy, M.-F., Diez-Guerra, F. J., Flores, J. M., Serrano, M., Auwerx, J., Diaz-Meco, M. T., & Moscat, J. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.011 · Cited by 290 · cited 4× · see citing works
“Conversely, tyrosine phosphorylation of both IRS-1 and its downstream target Akt in response to insulin injection was severely decreased in both muscle and fat tissues of p62 KO mice.(94) These results suggest that p62 may play a positive role in insulin sensitivity by enhancing the insulin signalling pathway, and p62…”
BackgroundInfluentialThe multifaceted role of mTORC1 in the control of lipid metabolism
Ricoult, S. J. H., & Manning, B. D. (2013) · EMBO Reports · doi:10.1038/embor.2013.5 · Cited by 287 · see citing works
Solinas, G., Naugler, W., Galimi, F., Lee, M.-S., & Karin, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607626103 · Cited by 284 · see citing works
Simonsen, A., Birkeland, H. C. G., Gillooly, D. J., Mizushima, N., Kuma, A., Yoshimori, T., Slagsvold, T., Brech, A., & Stenmark, H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01287 · Cited by 282 · see citing works
Pankiv, S., Lamark, T., Bruun, J., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.039925 · Cited by 266 · see citing works
Cardioprotection by resveratrol: a novel mechanism via autophagy involving the mTORC2 pathway
Gurusamy, N., Lekli, I., Mukherjee, S., Ray, D., Ahsan, M. K., Gherghiceanu, M., Popescu, L. M., & Das, D. K. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp384 · Cited by 263 · see citing works
Li, D., Wang, L. L., Deng, R., Tang, J., Shen, Y., Guo, J.-F., Wang, Y.-P., Xia, L.-P., Feng, G.-K., Liu, Q. Q., et al. (2008) · Oncogene · doi:10.1038/onc.2008.441 · Cited by 260 · see citing works
PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
Lazarou, M., Narendra, D. P., Jin, S. M., Tekle, E., Banerjee, S., & Youle, R. J. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201210111 · Cited by 247 · see citing works
p62: a versatile multitasker takes on cancer
Moscat, J., & Díaz-Meco, M. T. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.02.008 · Cited by 239 · see citing works
Sánchez‐Gómez, P., de Cárcer, G., Sandoval, I. V., Moscat, J., & Díaz-Meco, M. T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.3069 · Cited by 229 · see citing works
Selective turnover of p62/A170/SQSTM1 by autophagy
Ichimura, Y., Kominami, E., Tanaka, K., & Komatsu, M. (2008) · Autophagy · doi:10.4161/auto.6826 · Cited by 228 · see citing works
Wooten, M. W., Geetha, T., Seibenhener, M. L., Babu, J. R., Díaz-Meco, M. T., & Moscat, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500237200 · Cited by 225 · see citing works
Fujita, K.-I., Maeda, D., Xiao, Q., & Srinivasula, S. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014156108 · Cited by 225 · see citing works
Differential effects of JNK1 and JNK2 inhibition on murine steatohepatitis and insulin resistance†
Singh, R., Wang, Y., Xiang, Y., Tanaka, K. E., Gaarde, W. A., & Czaja, M. J. (2008) · Hepatology · doi:10.1002/hep.22578 · Cited by 224 · see citing works
Interaction of protein kinase C ζ with ZIP, a novel protein kinase C-binding protein
Puls, A., Schmidt, S., Grawe, F., & Stabel, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6191 · Cited by 213 · see citing works
Accumulation of p62/ SQSTM 1 is associated with poor prognosis in patients with lung adenocarcinoma
Inoue, D., Suzuki, T., Mitsuishi, Y., Miki, Y., Suzuki, S., Sugawara, S., Watanabe, M., Sakurada, A., Endo, C., Uruno, A., et al. (2012) · Cancer Science · doi:10.1111/j.1349-7006.2012.02216.x · Cited by 204 · see citing works
Cemma, M., Kim, P. K., & Brumell, J. H. (2011) · Autophagy · doi:10.4161/auto.7.3.14046 · Cited by 200 · see citing works
Midbody ring disposal by autophagy is a post-abscission event of cytokinesis
Pohl, C., & Jentsch, S. (2008) · Nature Cell Biology · doi:10.1038/ncb1813 · Cited by 197 · see citing works
Deubiquitinating enzyme CYLD negatively regulates RANK signaling and osteoclastogenesis in mice
Jin, W., Chang, M., Paul, E. M., Babu, G. R., Lee, A. J., Reiley, W. W., Wright, A., Zhang, M., You, J., & Sun, S. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34257 · Cited by 195 · see citing works
Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain.
Joung, I., Strominger, J. L., & Shin, J. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5991 · Cited by 194 · see citing works
Chronic Activation of mTOR Complex 1 Is Sufficient to Cause Hepatocellular Carcinoma in Mice
Menon, S., Yecies, J. L., Zhang, H., Howell, J. J., Nicholatos, J. W., Harputlugil, E., Bronson, R. T., Kwiatkowski, D. J., & Manning, B. D. (2012) · Science Signaling · doi:10.1126/scisignal.2002739 · Cited by 183 · see citing works
Thompson, H. G. R., Harris, J. W., Wold, B. J., Lin, F., & Brody, J. P. (2003) · Oncogene · doi:10.1038/sj.onc.1206325 · Cited by 181 · see citing works
p62 at the Interface of Autophagy, Oxidative Stress Signaling, and Cancer
Nezis, I. P., & Stenmark, H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4394 · Cited by 176 · see citing works
Ni, H., Boggess, N., McGill, M. R., Lebofsky, M., Borude, P. C., Apte, U. M., Jaeschke, H., & Ding, W. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs133 · Cited by 173 · see citing works
Self-citationSequestosome 1/p62 – More than just a scaffold
Seibenhener, M. L., Geetha, T., & Wooten, M. W. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.12.027 · Cited by 165 · see citing works
Riley, B. E., Kaiser, S. E., Shaler, T. A., Ng, A., Hara, T., Hipp, M. S., Lage, K., Xavier, R. J., Ryu, K., Taguchi, K., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201005012 · Cited by 162 · see citing works
Park, J. M., Huang, S., Wu, T., Foster, N. R., & Sinicrope, F. A. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.22954 · Cited by 153 · see citing works
P62 and the sequestosome, a novel mechanism for protein metabolism
Shin, J. (1998) · Archives of Pharmacal Research · doi:10.1007/bf02976748 · Cited by 146 · see citing works
Feedback on Fat: p62-mTORC1-Autophagy Connections
Moscat, J., & Díaz-Meco, M. T. (2011) · Cell · doi:10.1016/j.cell.2011.10.021 · Cited by 140 · see citing works
Parkin and Mitofusins Reciprocally Regulate Mitophagy and Mitochondrial Spheroid Formation
Ding, W., Guo, F., Ni, H., Bockus, A. B., Manley, S., Stolz, D. B., Eskelinen, E., Jaeschke, H., & Yin, X. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.413682 · Cited by 134 · see citing works
Self-citationKuusisto, E., Suuronen, T., & Salminen, A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4107 · Cited by 131 · see citing works
Harada, M., Hanada, S., Toivola, D. M., Ghori, N., & Omary, M. B. (2008) · Hepatology · doi:10.1002/hep.22294 · Cited by 126 · see citing works
PB1 Domain Interaction of p62/Sequestosome 1 and MEKK3 Regulates NF-κB Activation
Nakamura, K., Kimple, A. J., Siderovski, D. P., & Johnson, G. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.065102 · Cited by 125 · see citing works
p62 Links β-adrenergic input to mitochondrial function and thermogenesis
Müller, T. D., Lee, S. J., Jastroch, M., Kabra, D. G., Stemmer, K., Aichler, M., Abplanalp, B., Ananthakrishnan, G., Bhardwaj, N. J., Collins, S., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci64209 · Cited by 122 · see citing works
The Role of Ubiquitin in Autophagy-Dependent Protein Aggregate Processing
Yao, T. (2010) · Genes & Cancer · doi:10.1177/1947601910383277 · Cited by 121 · see citing works
Mallory–Denk-bodies: Lessons from keratin-containing hepatic inclusion bodies
Strnad, P., Zatloukal, K., Stumptner, C., Kulaksiz, H., & Denk, H. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.08.008 · Cited by 114 · see citing works
Park, I., Chung, J., Walsh, C. T., Yun, Y., Strominger, J. L., & Shin, J. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12338 · Cited by 112 · see citing works
A functional role for the p62–ERK1 axis in the control of energy homeostasis and adipogenesis
Lee, S. J., Pfluger, P. T., Kim, J. Y., Nogueiras, R., Durán, Á., Pagès, G., Pouysségur, J., Tschöp, M. H., Díaz-Meco, M. T., & Moscat, J. (2010) · EMBO Reports · doi:10.1038/embor.2010.7 · Cited by 108 · see citing works
Pan, J.-A., Ullman, E., Dou, Z., & Zong, W. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05460-11 · Cited by 108 · see citing works
Meerman, L., Koopen, N. R., Bloks, V. W., et al. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70464-6 · Cited by 101 · see citing works
Du, Y., Villeneuve, N. F., Wang, X., Sun, Z., Chen, W., Li, J., Lou, H., Wong, P. K., & Zhang, D. D. (2008) · Environmental Health Perspectives · doi:10.1289/ehp.11464 · Cited by 99 · see citing works
Hepatocellular Hyalin in Cholestasis and Cirrhosis: Its Diagnostic Significance
Gerber, M. A., Orr, W. C., Denk, H., et al. (1973) · Gastroenterology · doi:10.1016/s0016-5085(73)80095-2 · Cited by 93 · see citing works
Ishii, T., Yanagawa, T., Kawane, T., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1377 · Cited by 86 · see citing works
Analysis of Intracytoplasmic Hyaline Bodies in a Hepatocellular Carcinoma
Stumptner, C., Heid, H., Fuchsbichler, A., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65426-0 · Cited by 83 · see citing works
Moscat, J., Díaz-Meco, M. T., & Wooten, M. W. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.119 · Cited by 81 · see citing works
Müller, T., Langner, C., Fuchsbichler, A., Heinz‐Erian, P., Ellemunter, H., Schlenck, B., Bavdekar, A., Pradhan, A. M., Pandit, A., Müller‐Höcker, J., et al. (2004) · Hepatology · doi:10.1002/hep.20108 · Cited by 77 · see citing works
Vadlamudi, R. K., & Shin, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01021-7 · Cited by 71 · see citing works
The adaptor protein p62/SQSTM1 in osteoclast signaling pathways
McManus, S., & Roux, S. (2012) · Journal of Molecular Signaling · doi:10.1186/1750-2187-7-1 · Cited by 68 · see citing works
Recent advances in understanding the molecular basis of Paget disease of bone
Goode, A., & Layfield, R. (2009) · Journal of Clinical Pathology · doi:10.1136/jcp.2009.064428 · Cited by 68 · see citing works
Ishii, T., Yanagawa, T., Yuki, K., Kawane, T., Yoshida, H., & Bannai, S. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6221 · Cited by 67 · see citing works
Sasaki, M., Miyakoshi, M., Sato, Y., & Nakanuma, Y. (2011) · Liver International · doi:10.1111/j.1478-3231.2011.02656.x · Cited by 59 · see citing works
Stumptner, C., Fuchsbichler, A., Zatloukal, K., & Denk, H. (2007) · Hepatology · doi:10.1002/hep.21744 · Cited by 55 · see citing works
Sasaki, M., Miyakoshi, M., Sato, Y., & Nakanuma, Y. (2011) · Digestive Diseases and Sciences · doi:10.1007/s10620-011-1929-y · Cited by 48 · see citing works
Bile Acid-Induced Mallory Body Formation in Drug-Primed Mouse Liver
Fickert, P., Trauner, M. A., Fuchsbichler, A., Stumptner, C., Zatloukal, K., & Denk, H. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64480-x · Cited by 47 · see citing works
Ullman, E., Pan, J.-A., & Zong, W. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05452-11 · Cited by 44 · see citing works
The proteasome inhibitor, PS-341, causes cytokeratin aggresome formation
Bardag‐Gorce, F., Riley, N. E., Nan, L., et al. (2003) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2003.08.006 · Cited by 34 · see citing works
Tissue Specific Induction of p62/Sqstm1 by Farnesoid X Receptor
Williams, J. A. R., Thomas, A., Li, G., Kong, B., Zhan, L., Inaba, Y., Xie, W., Ding, W., & Guo, G. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043961 · Cited by 33 · see citing works
Self-citationSequestosome 1/p62, a Scaffolding Protein, Is a Newly Identified Partner of IRS-1 Protein
Geetha, T., Chen, Z., Vishwaprakash, N., Broderick, T. L., & Babu, J. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322404 · Cited by 31 · see citing works
Specific Regulation of Cytokine-Dependent p38 MAP Kinase Activation by p62/SQSTM1
Kawai, K., Saito, A., SUDO, T., & Osada, H. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvn027 · Cited by 26 · see citing works
Saito, A., Kawai, K., Takayama, H., SUDO, T., & Osada, H. (2008) · Chemistry - An Asian Journal · doi:10.1002/asia.200800099 · Cited by 21 · see citing works
Involvement of kinase PKC-zeta in the p62/p62P392L-driven activation of NF-κB in human osteoclasts
Chamoux, E., McManus, S., Laberge, G., Bisson, M., & Roux, S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.12.008 · Cited by 20 · see citing works
Griseofulvin-Induced Cholestasis in Swiss Albino Mice
Yokoo, H., Craig, R. M., Harwood, T. R., et al. (1979) · Gastroenterology · doi:10.1016/s0016-5085(79)80081-5 · Cited by 19 · see citing works
Cloning, Expression Profile, and Genomic Organization of the Mouse STAP/A170 Gene
Okazaki, M., Ito, S., Kawakita, K., Takeshita, S., Kawai, S., Makishima, F., Oda, H., & Kakinuma, A. (1999) · Genomics · doi:10.1006/geno.1999.5902 · Cited by 18 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [98]Muller TD Lee SJ Jastroch M Kabra D Stemmer K Aichler M Abplanalp B Ananthakrishnan G Bhardwaj N Collins S Divanovic S Endele M Finan B Gao Y Habegger KM Hembree J Heppner KM Hofmann S Holland J Kuchler D Kutschke M Krishna R Lehti M Oelkrug R Ottaway N Perez-Tilve D Raver C Walch AK Schriever SC Speakman J Tseng YH Diaz-Meco M Pfluger PT Moscat J Tschop MH p62 Links beta-adrenergic input to mitochondrial function and thermogenesis The Journal of clinical investigation 2012 PMC3533288 23257354
Cited by
Sorted by citations
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 · see citing works
“neural tissues manifest the detrimental effects of compromised autophagy [11], but to varying extents [365,366]: SQSTM1 mutations affect muscle, bone, and liver [125,367,368]; C9orf72 deficiency leads to lymphocytic inflammation, lymphadenopathy, and splenomegaly [149]; CHMP2B mutations induce oligodendroglial patholo…”
Background
- Authors
- Manley, S., Williams, J. A., & Ding, W.-X.
- Affiliations
- University of Kansas Medical Center (US)
- Corresponding author
- Ding, Wen-Xing
- Venue
- Experimental Biology and Medicine
- Publisher
- Frontiers Media SA
- Published
- 2013-05
- Volume
- 238
- Issue
- 5
- Pages
- 525-538
- ISSN
- 0071-3384 (ISSN-L)
- 1535-3702
- 1535-3699
- PMC
- PMC4096157
- OpenAlex
- W1983413606
- Cited by
- 135
- References
- 150
- Citations by year
- 2026: 1 · 2025: 9 · 2024: 11 · 2023: 11 · 2022: 9 · 2021: 9 · 2020: 13 · 2019: 9 · 2018: 14 · 2017: 13 · 2016: 13 · 2015: 11 · 2014: 10 · 2013: 2
- FWCI
- 7.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Experimental Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (R01AA020518, R37AA020518)
- National Institute of Environmental Health Sciences (T32ES007079)
- National Center for Research Resources (P20RR021940)
- Topics
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Epidemiology › Liver Disease Diagnosis and Treatment
- Keywords
- p62, liver physiology, liver disease pathogenesis, selective autophagy, autophagy receptors, protein aggregates, cholestasis, obesity, insulin resistance, hepatocyte death, NF-κB signaling, Nrf2 signaling, mTOR signaling, oxidative stress
- MeSH terms
- Sequestosome-1 Protein, Animals, Autophagy, Cell Transformation, Neoplastic, Inclusion Bodies, Humans, Inflammation, Insulin Resistance, Liver, Liver Neoplasms, Neoplasm Proteins, Signal Transduction, NF-kappa B, Oxidative Stress, Adaptor Proteins, Signal Transducing, Cell Proliferation, NF-E2-Related Factor 2, TOR Serine-Threonine Kinases
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