UBXD4, a UBX-Containing Protein, Regulates the Cell Surface Number and Stability of α3-Containing Nicotinic Acetylcholine Receptors
Open accessAbstract
Adaptor proteins are likely to modulate spatially and temporally the trafficking of a number of membrane proteins, including neuronal nicotinic acetylcholine receptors (nAChRs). A yeast two-hybrid screen identified a novel UBX-containing protein, UBXD4, as one of the cytosolic proteins that interact directly with the α3 and α4 nAChR subunits. The function of UBX-containing proteins is largely unknown. Immunoprecipitation and confocal microscopy confirmed the interaction of UBXD4 with α3-containing nAChRs (α3* nAChRs) expressed in HEK293 cells, PC12 cells, and rat cortical neurons. Overexpression of UBXD4 in differentiated PC12 cells (dPC12) increased nAChR cell surface expression, especially that of the α3β2 subtype. These findings were corroborated by electrophysiology, immunofluorescent staining, and biotinylation of surface receptors. Silencing of UBXD4 led to a significant reduction of α3* nAChRs in rat cortical neurons and dPC12 cells. Biochemical and immunofluorescence studies of endogenous UBXD4 showed that the protein is located in both the ER and cis-Golgi compartments. Our investigations also showed that the α3 subunit is ubiquitinated and that UBXD4 can interfere with its ubiquitination and consequent degradation by the proteasome. Our data suggest that UBXD4 modulates the distribution of α3* nAChRs between specialized intracellular compartments and the plasma membrane. This effect is achieved by controlling the stability of the α3 subunit and, consequently, the number of receptors at the cell surface.
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Cites
SMART, a simple modular architecture research tool: Identification of signaling domains
Schultz, J., Milpetz, F., Peer Bork, B., & Ponting, C. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5857 · Cited by 3,577 · see citing works
Amino Acid Sequences Common to Rapidly Degraded Proteins: The PEST Hypothesis
Rogers, S. W., Wells, R., & RECHSTEINER, M. C. (1986) · Science · doi:10.1126/science.2876518 · Cited by 2,565 · see citing works
Wada, E., Wada, K., Boulter, J., Deneris, E. S., Heinemann, S., Patrick, J., & Swanson, L. W. (1989) · The Journal of Comparative Neurology · doi:10.1002/cne.902840212 · Cited by 1,044 · see citing works
SMART 5: domains in the context of genomes and networks
Letunić, I. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj079 · Cited by 979 · see citing works
Ubiquitin and ubiquitin-like proteins as multifunctional signals
Welchman, R., Gordon, C., & Mayer, R. (2005) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1700 · Cited by 881 · see citing works
Polycystin-2 is an intracellular calcium release channel
Koulen, P., Cai, Y., Geng, L., Maeda, Y., Nishimura, S., Witzgall, R., Ehrlich, B. E., & Somlo, S. (2002) · Nature Cell Biology · doi:10.1038/ncb754 · Cited by 706 · see citing works
Hurley, J. H., Lee, S., & Prag, G. (2006) · Biochemical Journal · doi:10.1042/bj20061138 · Cited by 601 · see citing works
A statistical sampling algorithm for RNA secondary structure prediction
Ding, Y. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg938 · Cited by 566 · see citing works
Jensen, A. A., Frølund, B., Liljefors, T., & Krogsgaard‐Larsen, P. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm040219e · Cited by 541 · see citing works
ISOLATION OF RAT LIVER PLASMA MEMBRANES
Touster, O., Aronson, N. N., Dulaney, J. T., & Hendrickson, H. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.47.3.604 · Cited by 499 · see citing works
A New α-Conotoxin Which Targets α3β2 Nicotinic Acetylcholine Receptors
Cartier, G. E., Yoshikami, D., Gray, W. R., Luo, S., Olivera, B. M., & McIntosh, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7522 · Cited by 489 · see citing works
Self-citationVarshavsky, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90285-k · Cited by 469 · see citing works
p47 is a cofactor for p97-mediated membrane fusion
Kondo, H., Rabouille, C., Newman, R., Levine, T. P., Pappin, D., Freemont, P. S., & Warren, G. (1997) · Nature · doi:10.1038/40411 · Cited by 437 · see citing works
Le Novère, N., Corringer, P., & Changeux, J. (2002) · Journal of Neurobiology · doi:10.1002/neu.10153 · Cited by 411 · see citing works
The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
Hofmann, K., & Bücher, P. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30015-7 · Cited by 404 · see citing works
Assembly of Human Neuronal Nicotinic Receptor α5 Subunits with α3, β2, and β4 Subunits
Wang, F., Gerzanich, V., Wells, G. B., Anand, R., Peng, X.-D., Keyser, K. T., & Lindstrom, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17656 · Cited by 345 · see citing works
Self-citationChamptiaux, N., Han, Z., Bessis, A., Rossi, F., Zoli, M., Marubio, L. M., McIntosh, J. M., & Changeux, J. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-04-01208.2002 · Cited by 345 · see citing works
Self-citationDiverse polyubiquitin interaction properties of ubiquitin-associated domains
Raasi, S., Varadan, R., Fushman, D., & Pickart, C. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb962 · Cited by 335 · see citing works
RNA secondary structure prediction by centroids in a Boltzmann weighted ensemble
Ye, D., Chan, C. Y., & Lawrence, C. E. (2005) · RNA · doi:10.1261/rna.2500605 · Cited by 332 · see citing works
Braun, S. J., Matuschewski, K., Rapé, M., Thoms, S., & Jentsch, S. (2002) · The EMBO Journal · doi:10.1093/emboj/21.4.615 · Cited by 330 · see citing works
The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein
Özkaynak, E., Finley, D., & Varshavsky, A. J. (1984) · Nature · doi:10.1038/312663a0 · Cited by 310 · see citing works
UBXD7 Binds Multiple Ubiquitin Ligases and Implicates p97 in HIF1α Turnover
Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R., & Deshaies, R. J. (2008) · Cell · doi:10.1016/j.cell.2008.06.048 · Cited by 305 · see citing works
Vadlamudi, R. K., Joung, I., Strominger, J. L., & Shin, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20235 · Cited by 299 · see citing works
Gerzanich, V., Peng, X.-D., Wang, F., Wells, G. B., Anand, R., Fletcher, S. R., & Lindstrom, J. M. (1995) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10533-6 · Cited by 290 · see citing works
Self-citationXu, W., Gelber, S. E., Orr‐Urtreger, A., Armstrong, D. L., Lewis, R. A., Ou, C., Patrick, J. W., Role, L. W., Biasi, M. D., & Beaudet, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5746 · Cited by 287 · see citing works
Cdc48 (p97): a ‘molecular gearbox’ in the ubiquitin pathway?
Jentsch, S., & Rumpf, S. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.005 · Cited by 280 · see citing works
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
Schuberth, C. E., & Buchberger, A. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8072-8 · Cited by 277 · see citing works
Chi, N., & Lodish, H. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007635200 · Cited by 277 · see citing works
Berdon, W. E., Baker, D., Blanc, W., et al. (1976) · American Journal of Roentgenology · doi:10.2214/ajr.126.5.957 · Cited by 274 · see citing works
Raasi, S., & Pickart, C. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212841200 · Cited by 250 · see citing works
Bedford, F. K., Kittler, J. T., Muller, É., Thomas, P., Uren, J. M., Merlo, D., Wisden, W., Triller, A., Smart, T. G., & Moss, S. J. (2001) · Nature Neuroscience · doi:10.1038/nn0901-908 · Cited by 231 · see citing works
Salas, R., Pieri, F., & De Biasi, M. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1939-04.2004 · Cited by 226 · see citing works
Self-citationCui, C., Booker, T. K., Allen, R. S., Grady, S. R., Whiteaker, P., Marks, M. J., Salminen, O., Tritto, T., Butt, C. M., Allen, W. R., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-35-11045.2003 · Cited by 213 · see citing works
Self-citationAssembly and subunit diversity of nicotinic acetylcholine receptors
Millar, N. S. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310869 · Cited by 208 · see citing works
A Fas-associated protein factor, FAF1, potentiates Fas-mediated apoptosis.
Chu, K., Niu, X., & Williams, L. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11894 · Cited by 193 · see citing works
Wang, F., Nelson, M. E., Kuryatov, A., Olale, F., Cooper, J., Keyser, K., & Lindstrom, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28721 · Cited by 187 · see citing works
Self-citationFunctional cloning of TUG as a regulator of GLUT4 glucose transporter trafficking
Bogan, J. S., Hendon, N., McKee, A. E., Tsao, T., & Lodish, H. F. (2003) · Nature · doi:10.1038/nature01989 · Cited by 187 · see citing works
From UBA to UBX: new words in the ubiquitin vocabulary
Buchberger, A. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02269-9 · Cited by 175 · see citing works
Hamada, H., Suzuki, M., Yuasa, S., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8007-8017.2004 · Cited by 173 · see citing works
The expression of nicotinic acetylcholine receptors by PC12 cells treated with NGF
Rogers, S., Mandelzys, A., Deneris, E. S., Cooper, E. A., & Heinemann, S. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-12-04611.1992 · Cited by 162 · see citing works
Comparative Selectivity and Specificity of the Proteasome Inhibitors BzLLLCOCHO, PS-341, and MG-132
Crawford, L., WALKER, B. J., Ovaa, H., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0605 · Cited by 159 · see citing works
Lansdell, S. J., Gee, V. J., Harkness, P. C., Doward, A. I., Baker, E. R., Gibb, A. J., & Millar, N. S. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.017459 · Cited by 156 · see citing works
Wang, Y., Satoh, A., Warren, G., & Meyer, H. H. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401010 · Cited by 154 · see citing works
The Chaperone Protein 14-3-3η Interacts with the Nicotinic Acetylcholine Receptor α4 Subunit
Jeanclos, E. M., Lin, L., Treuil, M. W., Rao, J., DeCoster, M. A., & Anand, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011549200 · Cited by 154 · see citing works
Williams, M. E., Burton, B., Urrutia, A., Shcherbatko, A., Chavez-Noriega, L. E., Cohen, C. J., & Aiyar, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410039200 · Cited by 152 · see citing works
Marchand, S., Devillers‐Thiéry, A., Pons, S., Changeux, J., & Cartaud, J. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08891.2002 · Cited by 146 · see citing works
Gupta, D. S., McCullumsmith, R. E., Beneyto, M., Haroutunian, V., Davis, K. L., & Meador‐Woodruff, J. H. (2005) · Synapse · doi:10.1002/syn.20164 · Cited by 146 · see citing works
The UBX domain: a widespread ubiquitin-like module
Buchberger, A., Howard, M. J., Proctor, M., & Bycroft, M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4462 · Cited by 144 · see citing works
Le-Niculescu, H., Niesman, I. R., Fischer, T., DeVries, L., & Farquhar, M. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501833200 · Cited by 134 · see citing works
CARM1 Regulates Proliferation of PC12 Cells by Methylating HuD
Fujiwara, T., Mori, Y., Chu, D. L., Koyama, Y., Miyata, S., Tanaka, H., Yachi, K., Kubo, T., Yoshikawa, H., & Tohyama, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2273-2285.2006 · Cited by 130 · see citing works
Haynes, C. M., Caldwell, S. R., & Cooper, A. A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201053 · Cited by 122 · see citing works
A transmembrane motif governs the surface trafficking of nicotinic acetylcholine receptors
Wang, J.-M., Zhang, L., Yao, Y., Viroonchatapan, N., Rothe, E. E., & Wang, Z.-Z. (2002) · Nature Neuroscience · doi:10.1038/nn918 · Cited by 116 · see citing works
Salas, R., Cook, K. D., Bassetto, L., & De Biasi, M. (2004) · Neuropharmacology · doi:10.1016/j.neuropharm.2004.05.002 · Cited by 115 · see citing works
Self-citationNicotine regulates multiple synaptic proteins by inhibiting proteasomal activity
Rezvani, K., Teng, Y., Shim, D., & De Biasi, M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3353-07.2007 · Cited by 113 · see citing works
Self-citationFunctional α6-Containing Nicotinic Receptors Are Present in Chick Retina
Vailati, S., Hanke, W. R. L., Bejan, A., Barabino, B., Longhi, R., Balestra, B., Moretti, M., Clementi, F., & Gotti, C. (1999) · Molecular Pharmacology · doi:10.1124/mol.56.1.11 · Cited by 111 · see citing works
Surface and intracellular distribution of a putative neuronal nicotinic acetylcholine receptor.
Jacob, M. H., Lindstrom, J., & Berg, D. K. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.1.205 · Cited by 106 · see citing works
Self-citationLin, L., Jeanclos, E. M., Treuil, M. W., Braunewell, K., Gundelfinger, E. D., & Anand, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206857200 · Cited by 105 · see citing works
GAT (GGA and Tom1) Domain Responsible for Ubiquitin Binding and Ubiquitination
Shiba, Y., Katoh, Y., Shiba, T., Yoshino, K., Takatsu, H., Kobayashi, H., Shin, H., Soichi Wakatsuki, A., & Nakayama, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311702200 · Cited by 104 · see citing works
Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation
Liang, J., Yin, C., Doong, H., Fang, S., Peterhoff, C., Nixon, R. A., & Monteiro, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03163 · Cited by 97 · see citing works
Conroy, W. G., Liu, Z., Nai, Q., Coggan, J. S., & Berg, D. K. (2003) · Neuron · doi:10.1016/s0896-6273(03)00324-6 · Cited by 96 · see citing works
Regulation of Nicotinic Acetylcholine Receptor Assembly
Wanamaker, C., Christianson, J. C., & Green, W. N. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1254.009 · Cited by 95 · see citing works
Yu, C., Cresswell, J. A., Löffler, M. G., & Bogan, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610824200 · Cited by 90 · see citing works
Degradation Signals Recognized by the Ubc6p-Ubc7p Ubiquitin-Conjugating Enzyme Pair
Gilon, T., Chomsky, O., & Kulka, R. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7214-7219.2000 · Cited by 88 · see citing works
Yuan, X., Shaw, A., Zhang, X., Kondo, H., Lally, J., Freemont, P. S., & Matthews, S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4864 · Cited by 85 · see citing works
Jensen, A. A., Frølund, B., Liljefors, T., & Krogsgaard‐Larsen, P. (2005) · ChemInform · doi:10.1002/chin.200541286 · Cited by 84 · see citing works
A ‘distributed degron’ allows regulated entry into the ER degradation pathway
Gardner, R. G., & Hampton, R. Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5994 · Cited by 79 · see citing works
Keller, S. H., Lindstrom, J. M., Ellisman, M. H., & Taylor, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100691200 · Cited by 77 · see citing works
Self-citationNicotinic mechanisms in the autonomic control of organ systems
Biasi, M. D. (2002) · Journal of Neurobiology · doi:10.1002/neu.10145 · Cited by 74 · see citing works
Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes
Millard, S. M., & Wood, S. A. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200602082 · Cited by 71 · see citing works
Coupling Caspase Cleavage and Proteasomal Degradation of Proteins Carrying PEST Motif
Belizário, J. E., Alves, J. V., Garay-Malpartida, M., & Occhiucci, J. M. (2008) · Current Protein and Peptide Science · doi:10.2174/138920308784534023 · Cited by 66 · see citing works
Karan, G., Yang, Z., Howes, K. A., Zhao, Y., Chen, Y., Cameron, D. J., Lin, Y., Pearson, E., & Zhang, K. (2005) · PubMed · Cited by 65 · see citing works
Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human
Fukuda, M., OGATA, Y., Saegusa, C., Kanno, E., & Mikoshiba, K. (2002) · Biochemical Journal · doi:10.1042/bj20011877 · Cited by 63 · see citing works
Structural determinants of α4β2 nicotinic acetylcholine receptor trafficking
Ren, X.-Q., Cheng, S.-B., Treuil, M. W., Mukherjee, J., Rao, J., Braunewell, K. H., Lindstrom, J. M., & Anand, R. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1079-05.2005 · Cited by 61 · see citing works
Self-citationUbiquilin-1 Regulates Nicotine-induced Up-regulation of Neuronal Nicotinic Acetylcholine Receptors
Ficklin, M. B., Zhao, S., & Feng, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506781200 · Cited by 59 · see citing works
Saliba, R. S., Pangalos, M. N., & Moss, S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802077200 · Cited by 58 · see citing works
Wibo, M., Thinessempoux, D., Amar-Costesec, A., et al. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.89.3.456 · Cited by 57 · see citing works
Yeh, J. J., Yasuda, R. P., Dávila‐García, M. I., Xiao, Y., Ebert, S. N., Gupta, T., Kellar, K. J., & Wolfe, B. B. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.t01-1-00259.x · Cited by 52 · see citing works
Wanamaker, C., & Green, W. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705369200 · Cited by 51 · see citing works
The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
Hofmann, K. (1996) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(96)30015-7 · Cited by 51 · see citing works
Kassner, P. D., & Berg, D. K. (1997) · Journal of Neurobiology · doi:10.1002/(sici)1097-4695(199712)33:7 · Cited by 48 · see citing works
Determinants Responsible for Assembly of the Nicotinic Acetylcholine Receptor
Keller, S. H., & Taylor, P. (1999) · The Journal of General Physiology · doi:10.1085/jgp.113.2.171 · Cited by 47 · see citing works
Wanamaker, C., & Green, W. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501813200 · Cited by 46 · see citing works
Erbin Controls Dendritic Morphogenesis by Regulating Localization of δ-Catenin
Arikkath, J., Israely, I., Tao, Y., Mei, L., Liu, X., & Reichardt, L. F. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0451-08.2008 · Cited by 46 · see citing works
Ratnam, J., & Teichberg, V. I. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02936.x · Cited by 41 · see citing works
Analysis of TYA Protein Regions Necessary for Formation of the Ty1 Virus-like Particle Structure
Brookman, J. L., Stott, A. J., Cheeseman, P. J., et al. (1995) · Virology · doi:10.1006/viro.1995.1454 · Cited by 37 · see citing works
Trafficking and surface expression of the glutamate receptor subunit, KA2
Hayes, D. M., Braud, S., Hurtado, D. E., McCallum, J. D., Standley, S., Isaac, J. T. R., & Roche, K. W. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.115 · Cited by 34 · see citing works
Activation of p90Rsk1 Is Sufficient for Differentiation of PC12 Cells
Silverman, E., Frödin, M., Gammeltoft, S., & Maller, J. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10573-10583.2004 · Cited by 34 · see citing works
Characterization of the human β4 nAChR gene and polymorphisms in CHRNA3 and CHRNB4
Lev-Lehman, E., Bercovich, D., Xu, W., et al. (2001) · Journal of Human Genetics · doi:10.1007/pl00010921 · Cited by 30 · see citing works
Pons, S., Sallette, J., Bourgeois, J., Taly, A., Changeux, J., & Devillers‐Thiéry, A. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03673.x · Cited by 27 · see citing works
Wilson, J. D., Liu, Y., Bentivoglio, C. M., & Barlowe, C. K. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00460.x · Cited by 26 · see citing works
The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L
Soukenik, M., Diehl, A., Leidert, M., et al. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.037 · Cited by 19 · see citing works
Tettamanzi, M. C., Yu, C., Bogan, J. S., et al. (2006) · Protein Science · doi:10.1110/ps.051901806 · Cited by 18 · see citing works
NUB1‐mediated targeting of the ubiquitin precursor UbC1 for its C‐terminal hydrolysis
Tanaka, T., Yeh, E. T. H., & Kamitani, T. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.03999.x · Cited by 16 · see citing works
Wiser, M. F., & Schweiger, H. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90226-5 · Cited by 16 · see citing works
α-Synuclein expression localizes to the Golgi apparatus in bovine adrenal medullary chromaffin cells
Tompkins, M. M., Gai, W., Douglas, S. A., et al. (2003) · Brain Research · doi:10.1016/s0006-8993(03)03040-3 · Cited by 15 · see citing works
Arias, H., & Bhumireddy, P. (2005) · Current Protein and Peptide Science · doi:10.2174/138920305774329331 · Cited by 13 · see citing works
Protein phosphatases are pest containing proteins
Gomes, A. V., & Barnes, J. A. (1997) · IUBMB Life · doi:10.1080/15216549700201071 · Cited by 10 · see citing works
Kim, J., Yamaguchi, T., Sekine, S., et al. (1998) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022093 · Cited by 10 · see citing works
Srivatsan, M., TREECE, J., & Shotts, E. E. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1369.051 · Cited by 7 · see citing works
Detection of a surface-exposed PEST like sequence in the metabotropic glutamate receptor mGluR1 α
Soloviev, M. (2000) · Bioinformatics · doi:10.1093/bioinformatics/16.9.837 · Cited by 6 · see citing works
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“A variety of cellular processes influence receptor upregulation (Govind et al. 2009; Rezvani et al. 2009, 2010; Henderson et al. 2014).”
BackgroundSelf-citationMechanistic insights into nicotine withdrawal
Paolini, M., & De Biasi, M. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.075 · Cited by 66 · see citing works
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- Authors
- Rezvani, K., Teng, Y., Pan, Y., Dani, J. A., Lindstrom, J., García Gras, E. A., McIntosh, J. M., & De Biasi, M.
- Affiliations
- Baylor College of Medicine (US)
- University of Pennsylvania (US)
- University of Utah (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-05-27
- Volume
- 29
- Issue
- 21
- Pages
- 6883-6896
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2935801
- OpenAlex
- W2077314520
- Cited by
- 46
- References
- 100
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 2 · 2021: 2 · 2020: 1 · 2019: 3 · 2018: 1 · 2017: 2 · 2016: 4 · 2015: 9 · 2014: 5 · 2013: 6 · 2012: 2
- FWCI
- 1.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Philip Morris International
- National Institute of Mental Health (MH53631, R01MH053631, R29MH053631)
- National Institute on Drug Abuse (R21DA024385, DA017173, R01DA017173, R01DA009411)
- National Institute of Neurological Disorders and Stroke (R01NS021229)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- nicotinic acetylcholine receptors, alpha3 subunit, receptor trafficking, cell surface expression, receptor stability, ubiquitination, proteasomal degradation, adaptor proteins, cis-Golgi, endoplasmic reticulum, cortical neurons, PC12 cells
- MeSH terms
- Animals, Cell Differentiation, Cell Membrane, Cells, Cultured, Cerebral Cortex, Embryo, Mammalian, Endoplasmic Reticulum, Golgi Apparatus, Humans, Leucyl Aminopeptidase, Male, Membrane Potentials, Membrane Proteins, Mice, Inbred C57BL, Mutation, Neurons, Protein Binding, Receptors, Nicotinic, Transfection, Ubiquitins, Up-Regulation, Patch-Clamp Techniques, Microscopy, Confocal, Biotinylation, Rats, Long-Evans, Two-Hybrid System Techniques, RNA, Small Interfering, Proteasome Endopeptidase Complex, Immunoprecipitation, Mice, Rats
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 ›
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