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Journal of Biomedicine and Biotechnology
Volume 2006 (2006), Article ID 62079, 12 pages
Signaling, Polyubiquitination, Trafficking, and Inclusions: Sequestosome 1/p62's Role in Neurodegenerative Disease
Program in Cell & Molecular Biosciences, Department of Biological Sciences, Auburn University, Auburn, AL 36849, USA
Received 30 November 2005; Revised 20 February 2006; Accepted 27 February 2006
Copyright © 2006 Marie W. Wooten et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Citations to this Article [61 citations]
The following is the list of published articles that have cited the current article.
- Conny Stumptner, Andrea Fuchsbichler, Kurt Zatloukal, and Helmut Denk, “ In vitro production of Mallory bodies and intracellular hyaline bodies: The central role of sequestosome 1 / p62 ,” Hepatology, vol. 46, no. 3, pp. 851–860, 2007.
- Masaaki Komatsu, Satoshi Waguri, Masato Koike, Yu-shin Sou, Takashi Ueno, Taichi Hara, Noboru Mizushima, Jun-ichi Iwata, Junji Ezaki, Shigeo Murata, Jun Hamazaki, Yasumasa Nishito, Shun-ichiro Iemura, Tohru Natsume, Toru Yanagawa, Junya Uwayama, Eiji Warabi, Hiroshi Yoshida, Tetsuro Ishii, Akira Kobayashi, Masayuki Yamamoto, Zhenyu Yue, Yasuo Uchiyama, Eiki Kominami, and Keiji Tanaka, “Homeostatic Levels of p62 Control Cytoplasmic Inclusion Body Formation in Autophagy-Deficient Mice,” Cell, vol. 131, no. 6, pp. 1149–1163, 2007.
- Noboru Mizushima, “Autophagy: process and function,” Genes & Development, vol. 21, no. 22, pp. 2861–2873, 2007.
- Anna Janue, Montse Olive, and Isidre Ferrer, “Oxidative stress in desminopathies and myotilinopathies: A link between oxidative damage and abnormal protein aggregation,” Brain Pathology, vol. 17, no. 4, pp. 377–388, 2007.
- Greet Beyens, and Wim Van Hul, “Pathophysiology and genetics of metabolic bone disorders characterized by increased bone turnover,” Critical Reviews In Eukaryotic Gene Expression, vol. 17, no. 3, pp. 215–240, 2007.
- A. Aigelsreiter, E. Janig, C. Stumptner, A. Fuchsbichler, K. Zatloukal, and H. Denk, “How a cell deals with abnormal proteins,” Pathobiology, vol. 74, no. 3, pp. 145–158, 2007.
- Masanori Hiji, Tetsuya Takahashi, Hiromasa Fukuba, Hiroshi Yamashita, Tatsuo Kohriyama, and Masayasu Matsumoto, “White matter lesions in the brain with frontotemporal lobar degeneration with motor neuron disease: TDP-43-immunopositive inclusions co-localize with p62, but not ubiquitin,” Acta Neuropathologica, vol. 116, no. 2, pp. 183–191, 2008.
- Miep H. Helfrich, and Lynne J. Hocking, “Genetics and aetiology of Pagetic disorders of bone,” Archives of Biochemistry and Biophysics, vol. 473, no. 2, pp. 172–182, 2008.
- Yasuo Uchiyama, Masahiro Shibata, Masato Koike, Kentaro Yoshimura, and Mitsuho Sasaki, “Autophagy-physiology and pathophysiology,” Histochemistry and Cell Biology, vol. 129, no. 4, pp. 407–420, 2008.
- E. Kuusisto, T. Kauppinen, and I. Alafuzoff, “Use of p62/SQSTM1 antibodies for neuropathological diagnosis,” Neuropathology and Applied Neurobiology, vol. 34, no. 2, pp. 169–180, 2008.
- Maria Pikkarainen, Päivi Hartikainen, and Irina Alafuzoff, “Neuropathologic features of frontotemporal lobar degeneration with ubiquitin-positive inclusions visualized with ubiquitin-binding protein p62 immunohistochemistry,” Journal of Neuropathology and Experimental Neurology, vol. 67, no. 4, pp. 280–298, 2008.
- Julie P. M. Viala, Sofia N. Mochegova, Nicole Meyer-Morse, and Daniel A. Portnoy, “A bacterial pore-forming toxin forms aggregates in cells that resemble those associated with neurodegenerative diseases,” Cellular Microbiology, vol. 10, no. 4, pp. 985–993, 2008.
- Ioannis P. Nezis, Anne Simonsen, Antonia P. Sagona, Kim Finley, Sébastien Gaumer, Didier Contamine, Tor Erik Rusten, Harald Stenmark, and Andreas Brech, “Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain,” Journal of Cell Biology, vol. 180, no. 6, pp. 1065–1071, 2008.
- Andrew Y. Gracey, Maxine L. Chaney, Judson P. Boomhower, William R. Tyburczy, Kwasi Connor, and George N. Somero, “Rhythms of Gene Expression in a Fluctuating Intertidal Environment,” Current Biology, vol. 18, no. 19, pp. 1501–1507, 2008.
- Kurt A. Jellinger, “Recent advances in our understanding of neurodegeneration,” Journal of Neural Transmission, vol. 116, no. 9, pp. 1111–1162, 2009.
- Maria J. Casarejos, Rosa M. Solano, José A. Rodriguez-Navarro, Ana Gómez, Juan Perucho, Jose G. Castaño, Justo García de Yébenes, and Maria A. Mena, “Parkin deficiency increases the resistance of midbrain neurons and glia to mild proteasome inhibition: the role of autophagy and glutathione homeostasis,” Journal of Neurochemistry, vol. 110, no. 5, pp. 1523–1537, 2009.
- Yifeng Du, Michael C. Wooten, and Marie W. Wooten, “Oxidative damage to the promoter region of SQSTM1/p62 is common to neurodegenerative disease,” Neurobiology of Disease, vol. 35, no. 2, pp. 302–310, 2009.
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- Viktor I. Korolchuk, Alicia Mansilla, Fiona M. Menzies, and David C. Rubinsztein, “Autophagy Inhibition Compromises Degradation of Ubiquitin-Proteasome Pathway Substrates,” Molecular Cell, vol. 33, no. 4, pp. 517–527, 2009.
- J. I-Ju Leu, Julia Pimkina, Amanda Frank, Maureen E. Murphy, and Donna L. George, “A Small Molecule Inhibitor of Inducible Heat Shock Protein 70,” Molecular Cell, vol. 36, no. 1, pp. 15–27, 2009.
- J-P Pursiheimo, K. Rantanen, P. T. Heikkinen, T. Johansen, and P. M. Jaakkola, “Hypoxia-activated autophagy accelerates degradation of SQSTM1/p62,” Oncogene, vol. 28, no. 3, pp. 334–344, 2009.
- Noboru Mizushima, “Physiological functions of autophagy,” Current Topics in Microbiology and Immunology, vol. 335, no. 1, pp. 71–84, 2009.
- Akiko Kuma, and Noboru Mizushima, “Physiological role of autophagy as an intracellular recycling system: With an emphasis on nutrient metabolism,” Seminars in Cell & Developmental Biology, vol. 21, no. 7, pp. 683–690, 2010.
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- Andrew King, Satomi Maekawa, Istvan Bodi, Claire Troakes, and Safa Al-Sarraj, “Ubiquitinated, p62 immunopositive cerebellar cortical neuronal inclusions are evident across the spectrum of TDP-43 proteinopathies but are only rarely additionally immunopositive for phosphorylation-dependent TDP-43,” Neuropathology, vol. 31, no. 3, pp. 239–249, 2010.
- Cyntia Curcio-Morelli, Florie A. Charles, Matthew C. Micsenyi, Yi Cao, Bhuvarahamurthy Venugopal, Marsha F. Browning, Kostantin Dobrenis, Susan L. Cotman, Steven U. Walkley, and Susan A. Slaugenhaupt, “Macroautophagy is defective in mucolipin-1-deficient mouse neurons,” Neurobiology of Disease, vol. 40, no. 2, pp. 370–377, 2010.
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- Qian Huang, and Maria E. Figueiredo-Pereira, “Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications,” Apoptosis, vol. 15, no. 11, pp. 1292–1311, 2010.
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- Andreas Urbanczyk, and Ralf Enz, “Spartin recruits PKC-ζ via the PKC-ζ-interacting proteins ZIP1 and ZIP3 to lipid droplets,” Journal of Neurochemistry, vol. 118, no. 5, pp. 737–748, 2011.
- Natura Myeku, and Maria E. Figueiredo-Pereira, “Dynamics of the Degradation of Ubiquitinated Proteins by Proteasomes and Autophagy ASSOCIATION WITH SEQUESTOSOME 1/p62,” Journal Of Biological Chemistry, vol. 286, no. 25, pp. 22426–22440, 2011.
- M. J. Casarejos, R. M. Solano, A. Gomez, J. Perucho, J. G. de Yebenes, and M. A. Mena, “The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells,” Neurochemistry International, vol. 58, no. 4, pp. 512–520, 2011.
- Thomas Weide, and Tobias B. Huber, “Implications of autophagy for glomerular aging and disease,” Cell and Tissue Research, vol. 343, no. 3, pp. 467–473, 2011.
- J. F. Rivera, T. Gurlo, M. Daval, C. J. Huang, A. V. Matveyenko, P. C. Butler, and S. Costes, “Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic beta-cells: protective role of p62-positive cytoplasmic inclusions,” Cell Death And Differentiation, vol. 18, no. 3, pp. 415–426, 2011.
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- Eisuke Itakura, and Noboru Mizushima, “p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding,” Journal Of Cell Biology, vol. 192, no. 1, pp. 17–27, 2011.
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- K. Seidel, M. Meister, G. J. Dugbartey, M. P. Zijlstra, J. Vinet, E. R. P. Brunt, F. W. van Leeuwen, U. Rüb, H. H. Kampinga, and W. F. A. den Dunnen, “Cellular protein quality control and the evolution of aggregates in spinocerebellar ataxia type 3 (SCA3),” Neuropathology and Applied Neurobiology, vol. 38, no. 6, pp. 548–558, 2012.
- Eric B. Dammer, Gary J. Bassell, Nicholas T. Seyfried, Claudia Fallini, Yair M. Gozal, Duc M. Duong, Wilfried Rossoll, Ping Xu, James J. Lah, Allan I. Levey, and Junmin Peng, “Coaggregation of RNA-binding proteins in a model of TDP-43 proteinopathy with selective RGG motif methylation and a role for RRM1 ubiquitination,” PLoS ONE, vol. 7, no. 6, 2012.
- Johannes Brettschneider, Vivianna M. Van Deerlin, John L. Robinson, Linda Kwong, Edward B. Lee, Yousuf O. Ali, Nathaniel Safren, Mervyn J. Monteiro, Jon B. Toledo, Lauren Elman, Leo McCluskey, David J. Irwin, Murray Grossman, Laura Molina-Porcel, Virginia M. -Y. Lee, and John Q. Trojanowski, “Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion,” Acta Neuropathologica, vol. 123, no. 6, pp. 825–839, 2012.
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- Yin Xu, Chan Tian, Shao-Bin Wang, Wu-Ling Xie, Yan Guo, Jin Zhang, Qi Shi, Cao Chen, and Xiao-Ping Dong, “Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases,” Autophagy, vol. 8, no. 11, pp. 1604–1620, 2012.
- Natura Myeku, Hu Wang, and Maria E. Figueiredo-Pereira, “cAMP stimulates the ubiquitin/proteasome pathway in rat spinal cord neurons,” Neuroscience Letters, vol. 527, no. 2, pp. 126–131, 2012.
- Stephen McManus, and Sophie Roux, “The adaptor protein p62/SQSTM1 in osteoclast signaling pathways,” Journal of Molecular Signaling, vol. 7, 2012.
- Marc Cruts, Ilse Gijselinck, Tim Van Langenhove, Julie van der Zee, and Christine Van Broeckhoven, “Current insights into the C9orf72 repeat expansion diseases of the FTLD/ALS spectrum,” Trends in Neurosciences, 2013.
- Takuya Konno, Masatoyo Nishizawa, Hitoshi Takahashi, Osamu Onodera, Atsushi Shiga, Akira Tsujino, Akihiro Sugai, Taisuke Kato, Kazuaki Kanai, Akio Yokoseki, Hiroto Eguchi, and Satoshi Kuwabara, “Japanese amyotrophic lateral sclerosis patients with GGGGCC hexanucleotide repeat expansion in C9ORF72,” Journal of Neurology, Neurosurgery and Psychiatry, vol. 84, no. 4, pp. 398–401, 2013.
- Amandine Magnaudeix, Cornelia M. Wilson, Guylène Page, Chantal Bauvy, Patrice Codogno, Philippe Lévêque, François Labrousse, Manuela Corre-Delage, Catherine Yardin, and Faraj Terro, “PP2A blockade inhibits autophagy and causes intraneuronal accumulation of ubiquitinated proteins,” Neurobiology of Aging, vol. 34, no. 3, pp. 770–790, 2013.
- M. Lamar Seibenhener, Yifeng Du, Maria-Theresa Diaz-Meco, Jorge Moscat, Michael C. Wooten, and Marie W. Wooten, “A role for sequestosome 1/p62 in mitochondrial dynamics, import and genome integrity,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol. 1833, no. 3, pp. 452–459, 2013.
- Heiko Braak, Dietmar Rudolf Thal, Jakob Matschke, Estifanos Ghebremedhin, and Kelly Del Tredici, “Age-related appearance of dendritic inclusions in catecholaminergic brainstem neurons,” Neurobiology of Aging, vol. 34, no. 1, pp. 286–297, 2013.
- Sarah L. Rea, John P. Walsh, Thomas Ratajczak, Jiake Xu, and Robert Layfield, “New Insights Into the Role of Sequestosome 1/p62 Mutant Proteins in the Pathogenesis of Paget's Disease of Bone,” Endocrine Reviews, vol. 34, no. 4, pp. 501–524, 2013.
- Jakub Sikora, Matthew C. Micsenyi, Kostantin Dobrenis, Gloria Stephney, and Steven U. Walkley, “Lysosomal Membrane Permeability Stimulates Protein Aggregate Formation in Neurons of a Lysosomal Disease,” Journal Of Neuroscience, vol. 33, no. 26, pp. 10815–10827, 2013.
- Gabor G. Kovacs, Homa Adle-Biassette, Ivan Milenkovic, Sara Cipriani, Jackelien van Scheppingen, and Eleonora Aronica, “Linking pathways in the developing and ageing brain with neurodegeneration,” Neuroscience, 2014.
- Mayurbhai Himatbhai Sahani, Eisuke Itakura, and Noboru Mizushima, “Expression of the autophagy substrate SQSTM1/p62 is restored during prolonged starvation depending on transcriptional upregulation and autophagy-derived amino acids,” Autophagy, vol. 10, no. 3, pp. 431–441, 2014.
- Aaron Y. Lai, Cynthia P. Lan, Salwa Hasan, and Mary E. Brown, “scyllo-Inositol Promotes Robust Mutant Huntingtin Protein Degradation,” Journal of Biological Chemistry, vol. 289, no. 6, pp. 3666–3676, 2014.
- Irving M Shapiro, Robert Layfield, Martin Lotz, Carmine Settembre, and Caroline Whitehouse, “Boning up on autophagy: The role of autophagy in skeletal biology,” Autophagy, vol. 10, no. 1, pp. 7–19, 2014.