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A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function
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The neuronal proteasome associates with plasma membranes.
“The neuronal proteasome also associates with plasma membranes (Ramachandran and Margolis, 2017), offering another possible neuron-specific site of convergence between CE and the proteasome.”
From Cholesterol Metabolism Is a Druggable Axis that Independently Regulates Tau and Amyloid-β in iPSC-Derived Alzheimer’s Disease Neurons (2019) · cites this paper as Ramachandran and Margolis, 2017
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Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875
Long-Term Potentiation--A Decade of Progress?
Malenka, R. C., & Nicoll, A. R. A. (1999) · Science · doi:10.1126/science.285.5435.1870 · Cited by 2,729
Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
Ehlers, M. D. (2003) · Nature Neuroscience · doi:10.1038/nn1013 · Cited by 977
Gene essentiality and synthetic lethality in haploid human cells
Blomen, V. A., Májek, P., Jae, L. T., Bigenzahn, J. W., Nieuwenhuis, J., Staring, J., Sacco, R., van Diemen, F. R., Olk, N., Stukalov, A., et al. (2015) · Science · doi:10.1126/science.aac7557 · Cited by 857
Functional requirement for class I MHC in CNS development and plasticity
Huh, G. S., Boulanger, L. M., Du, H., Riquelme, P. A., Brotz, T. M., & Shatz, C. J. (2000) · Science · doi:10.1126/science.290.5499.2155 · Cited by 828
Kim, M. J., Dunah, A. W., Wang, Y. T., & Sheng, M. (2005) · Neuron · doi:10.1016/j.neuron.2005.04.031 · Cited by 494
Increased proteasome activity in human embryonic stem cells is regulated by PSMD11
Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., et al. (2012) · Nature · doi:10.1038/nature11468 · Cited by 388
Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
Bingol, B., & Schuman, E. M. (2006) · Nature · doi:10.1038/nature04769 · Cited by 347
Margolis, S. S., Salogiannis, J., Lipton, D. M., Mandel-Brehm, C., Wills, Z. P., Mardinly, A. R., Hu, L., Greer, P. L., Bikoff, J. B., Ho, H.-Y. H., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.038 · Cited by 256
Self-citationRegulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
Djakovic, S. N., Schwarz, L. A., Barylko, B., DeMartino, G. N., & Patrick, G. N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021956 · Cited by 236
Dong, C., Upadhya, S. C., Ding, L., Smith, T. K., & Hegde, A. N. (2008) · Learning & Memory · doi:10.1101/lm.984508 · Cited by 158
Flagged first, then by citations
Research works printed but not linked: 47
- Coux, O., Tanaka, K. & Goldberg, A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801–847 (1996). · DOI
- Ciechanover, A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17, 7151–7160 (1998). · DOI
- Ciechanover, A. & Schwartz, A.L. The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death. Proc. Natl. Acad. Sci. USA 95, 2727–2730 (1998). · DOI
- Ben-Nissan, G. & Sharon, M. Regulating the 20S proteasome ubiquitin-independent degradation pathway. Biomolecules 4, 862–884 (2014). · DOI
- Kisselev, A.F., van der Linden, W.A. & Overkleeft, H.S. Proteasome inhibitors: an expanding army attacking a unique target. Chem. Biol. 19, 99–115 (2012). · DOI
- Wang, H.R. et al. Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302, 1775–1779 (2003). · DOI · Paper page
- Karpova, A., Mikhaylova, M., Thomas, U., Knöpfel, T. & Behnisch, T. Involvement of protein synthesis and degradation in long-term potentiation of Schaffer collateral CA1 synapses. J. Neurosci. 26, 4949–4955 (2006). · DOI
- Cai, F., Frey, J.U., Sanna, P.P. & Behnisch, T. Protein degradation by the proteasome is required for synaptic tagging and the heterosynaptic stabilization of hippocampal late-phase long-term potentiation. Neuroscience 169, 1520–1526 (2010). · DOI
- Rinetti, G.V. & Schweizer, F.E. Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons. J. Neurosci. 30, 3157–3166 (2010). · DOI
- Wu, S. et al. Cellular calcium deficiency plays a role in neuronal death caused by proteasome inhibitors. J. Neurochem. 109, 1225–1236 (2009). · DOI
- Fonseca, R., Vabulas, R.M., Hartl, F.U., Bonhoeffer, T. & Nägerl, U.V. A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron 52, 239–245 (2006). · DOI · Paper page
- Pines, J. & Lindon, C. Proteolysis: anytime, any place, anywhere? Nat. Cell Biol. 7, 731–735 (2005). · DOI
- Asano, S. et al. Proteasomes. A molecular census of 26S proteasomes in intact neurons. Science 347, 439–442 (2015). · DOI
- Patrick, G.N., Bingol, B., Weld, H.A. & Schuman, E.M. Ubiquitin-mediated proteasome activity is required for agonist-induced endocytosis of GluRs. Curr. Biol. 13, 2073–2081 (2003). · DOI
- van Weering, J.R. et al. Intracellular membrane traffic at high resolution. Methods Cell Biol. 96, 619–648 (2010). · DOI
- Chen, X. et al. PSD-95 family MAGUKs are essential for anchoring AMPA and NMDA receptor complexes at the postsynaptic density. Proc. Natl. Acad. Sci. USA 112, E6983–E6992 (2015). · DOI · Paper page
- Gazula, V.R. et al. Localization of Kv1.3 channels in presynaptic terminals of brainstem auditory neurons. J. Comp. Neurol. 518, 3205–3220 (2010). · DOI
- Hanley, J.G., Khatri, L., Hanson, P.I. & Ziff, E.B. NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex. Neuron 34, 53–67 (2002). · DOI
- Peebles, C.L. et al. Arc regulates spine morphology and maintains network stability in vivo. Proc. Natl. Acad. Sci. USA 107, 18173–18178 (2010). · DOI · Paper page
- Lin, D.T. et al. Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation. Nat. Neurosci. 12, 879–887 (2009). · DOI · Paper page
- Ehlers, M.D. Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron 28, 511–525 (2000). · DOI · Paper page
- Caterina, M.J., Hereld, D. & Devreotes, P.N. Occupancy of the Dictyostelium cAMP receptor, cAR1, induces a reduction in affinity which depends upon COOH-terminal serine residues. J. Biol. Chem. 270, 4418–4423 (1995). · DOI
- Zhu, P.P. et al. Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin. J. Biol. Chem. 278, 49063–49071 (2003). · DOI
- Wunder, C., Lippincott-Schwartz, J. & Lorenz, H. Determining membrane protein topologies in single cells and high-throughput screening applications. Curr. Protoc. Cell Biol. Chapter 5, Unit 5.7 (2010). · DOI
- Lee, Y.C., Srajer Gajdosik, M., Josic, D. & Lin, S.H. Plasma membrane isolation using immobilized concanavalin A magnetic beads. Methods Mol. Biol. 909, 29–41 (2012). · DOI
- Smith, M.J. & Koch, G.L. Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J. 8, 3581–3586 (1989). · DOI
- Park, S. et al. GDE2 promotes neurogenesis by glycosylphosphatidylinositol-anchor cleavage of RECK. Science 339, 324–328 (2013). · DOI · Paper page
- Besche, H.C., Haas, W., Gygi, S.P. & Goldberg, A.L. Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins. Biochemistry 48, 2538–2549 (2009). · DOI
- Werner, H., Dimou, L., Klugmann, M., Pfeiffer, S. & Nave, K.A. Multiple splice isoforms of proteolipid M6B in neurons and oligodendrocytes. Mol. Cell. Neurosci. 18, 593–605 (2001). · DOI
- Fuchsova, B., Fernández, M.E., Alfonso, J. & Frasch, A.C. Cysteine residues in the large extracellular loop (EC2) are essential for the function of the stress-regulated glycoprotein M6a. J. Biol. Chem. 284, 32075–32088 (2009). · DOI
- Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770–774 (2000). · DOI
- Kisselev, A.F., Akopian, T.N. & Goldberg, A.L. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273, 1982–1989 (1998). · DOI
- Li, N. et al. Relative quantification of proteasome activity by activity-based protein profiling and LC-MS/MS. Nat. Protoc. 8, 1155–1168 (2013). · DOI
- Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96, 10403–10408 (1999). · DOI
- Patel, T.P., Man, K., Firestein, B.L. & Meaney, D.F. Automated quantification of neuronal networks and single-cell calcium dynamics using calcium imaging. J. Neurosci. Methods 243, 26–38 (2015). · DOI
- Sato, Y., Watanabe, N., Fukushima, N., Mita, S. & Hirata, T. Actin-independent behavior and membrane deformation exhibited by the four-transmembrane protein M6a. PLoS One 6, e26702 (2011). · DOI
- Besche, H.C. & Goldberg, A.L. Affinity purification of mammalian 26S proteasomes using an ubiquitin-like domain. Methods Mol. Biol. 832, 423–432 (2012). · DOI · Paper page
- Tai, H.C. & Schuman, E.M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 9, 826–838 (2008). · DOI · Paper page
- Tsvetkov, P. et al. Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome. Proteins 70, 1357–1366 (2008). · DOI
- Tsvetkov, P., Reuven, N., Prives, C. & Shaul, Y. Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response. J. Biol. Chem. 284, 26234–26242 (2009). · DOI
- Schmidt, M. & Finley, D. Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 1843, 13–25 (2014). · DOI
- Jiang, S., Dupont, N., Castillo, E.F. & Deretic, V. Secretory versus degradative autophagy: unconventional secretion of inflammatory mediators. J. Innate Immun. 5, 471–479 (2013). · DOI · Paper page
- Lee, J.G., Takahama, S., Zhang, G., Tomarev, S.I. & Ye, Y. Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells. Nat. Cell Biol. 18, 765–776 (2016). · DOI
- Shatz, C.J. MHC class I: an unexpected role in neuronal plasticity. Neuron 64, 40–45 (2009). · DOI
- Xia, Z., Dudek, H., Miranti, C.K. & Greenberg, M.E. Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism. J. Neurosci. 16, 5425–5436 (1996). · DOI
- Nicoll, R.A. & Roche, K.W. Long-term potentiation: peeling the onion. Neuropharmacology 74, 18–22 (2013). · DOI
- Kim, Y.S. et al. Central terminal sensitization of TRPV1 by descending serotonergic facilitation modulates chronic pain. Neuron 81, 873–887 (2014). · DOI
Cited by
Sorted by citations
van der Kant, R., Langness, V. F., Herrera, C. M., Williams, D. A., Fong, L. K., Leestemaker, Y., Steenvoorden, E., Rynearson, K. D., Brouwers, J. F., Helms, J. B., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.12.013 · Cited by 350
Fricker, L. D. (2020) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010919-023603 · Cited by 309
Metadata
- Authors
- Ramachandran, K. V., & Margolis, S. S.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2017-03-13
- Volume
- 24
- Issue
- 4
- Pages
- 419-430
- ISSN
- 1545-9993
- 1545-9985
- PMC
- PMC5383508
- Cited by
- 151
- References
- 11
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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