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Ubiquitination and the Regulation of Membrane Proteins

Foot, Natalie, Henshall, Tanya, Kumar, Sharad·2017·Physiological Reviews

DOI 10.1152/physrev.00012.2016

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Abstract

Newly synthesized transmembrane proteins undergo a series of steps to ensure that only the required amount of correctly folded protein is localized to the membrane. The regulation of protein quality and its abundance at the membrane are often controlled by ubiquitination, a multistep enzymatic process that results in the attachment of ubiquitin, or chains of ubiquitin to the target protein. Protein ubiquitination acts as a signal for sorting, trafficking, and the removal of membrane proteins via endocytosis, a process through which multiple ubiquitin ligases are known to specifically regulate the functions of a number of ion channels, transporters, and signaling receptors. Endocytic removal of these proteins through ubiquitin-dependent endocytosis provides a way to rapidly downregulate the physiological outcomes, and defects in such controls are directly linked to human pathologies. Recent evidence suggests that ubiquitination is also involved in the shedding of membranes and associated proteins as extracellular vesicles, thereby not only controlling the cell surface levels of some membrane proteins, but also their potential transport to neighboring cells. In this review, we summarize the mechanisms and functions of ubiquitination of membrane proteins and provide specific examples of ubiquitin-dependent regulation of membrane proteins.

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Extracellular vesicles: Exosomes, microvesicles, and friends
Raposo, G., & Stoorvogel, W. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211138 · Cited by 8,099
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes)
Johnstone, R. M., Adam, M., Hammond, J. R., Orr, L., & Turbide, C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48095-7 · Cited by 2,931
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Function and regulation of cullin–RING ubiquitin ligases
Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · cited 1×
“This removal of mitochondrial proteins then leads to the degradation of the mitochondria by mitophagy (41, 340).”
Background
FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806

Show all 25 references

Research works printed but not linked: 366

10.3324/haematol.13187 · DOI
10.1172/JCI5713 · DOI · Paper page
10.1152/physiol.00033.2005 · DOI
10.1074/jbc.M513803200 · DOI
10.1038/nn.3120 · DOI
10.1016/S0014-5793(00)01621-5 · DOI
10.3109/09687688.2015.1023378 · DOI
10.1074/jbc.M115.675579 · DOI
10.3748/wjg.14.6863 · DOI
10.1186/1471-2148-8-222 · DOI · Paper page
10.1038/labinvest.2010.152 · DOI · Paper page
10.1016/j.neuron.2006.03.044 · DOI · Paper page
10.1681/ASN.2011020132 · DOI · Paper page
10.1074/jbc.M113.515056 · DOI
10.1016/j.biocel.2009.10.005 · DOI
10.1128/JVI.78.3.1109-1120.2004 · DOI · Paper page
10.1038/35050524 · DOI · Paper page
10.1016/j.bbrc.2015.08.099 · doi:10.1016/j.bbrc.2015.08.099
10.1091/mbc.E09-11-0926 · DOI
10.1074/jbc.M110.129411 · DOI
10.1091/mbc.E08-03-0308 · DOI
10.1091/mbc.E03-04-0202 · DOI
10.1016/j.gene.2014.12.020 · DOI · Paper page
10.1038/ncomms1284 · DOI
10.1091/mbc.11.4.1241 · DOI · Paper page
10.1038/nrm1279 · DOI · Paper page
10.1074/jbc.M508632200 · DOI · Paper page
10.1038/nature10814 · DOI · Paper page
10.1128/JVI.00307-10 · DOI · Paper page
10.1016/S0896-6273(02)00749-3 · DOI · Paper page
10.1182/blood-2006-12-061176 · DOI
10.1126/scisignal.1160940 · DOI · Paper page
Caohuy H, 2014, J Biol Chem, 289, 35953, 10.1074/jbc.M114.598649 · DOI
10.1038/nature08130 · DOI
10.1242/dev.015529 · DOI
10.1523/JNEUROSCI.1817-09.2009 · DOI
10.1016/j.cell.2006.05.043 · DOI · Paper page
10.1093/hmg/11.23.2895 · DOI · Paper page
10.1093/hmg/ddr048 · DOI · Paper page
10.1371/journal.pone.0002735 · DOI
10.1158/1535-7163.MCT-04-0338 · DOI · Paper page
10.1158/1078-0432.CCR-11-0476 · DOI · Paper page
10.1128/MCB.00407-09 · DOI
10.1034/j.1600-0854.2002.030204.x · DOI
10.1016/j.ydbio.2003.11.010 · DOI
10.1042/CS20150511 · DOI
10.1042/BST0380144 · DOI
10.1002/dvdy.20683 · DOI
10.1038/nsmb.2793 · DOI · Paper page
10.4161/cib.23094 · DOI
10.1016/j.tcb.2015.03.002 · DOI · Paper page
10.1016/j.tcb.2006.09.002 · DOI · Paper page
10.1146/annurev-cellbio-101512-122326 · DOI · Paper page
10.1038/cdd.2010.130 · DOI
10.1242/jcs.131250 · DOI
10.1016/S1534-5807(01)00091-0 · DOI · Paper page
10.1038/emboj.2011.224 · DOI
10.1038/35086595 · DOI · Paper page
10.1128/MCB.23.15.5331-5345.2003 · DOI
10.1074/jbc.M109.049411 · DOI
10.1073/pnas.95.12.7169 · DOI
10.1091/mbc.E15-05-0284 · DOI
10.1124/mol.112.079418 · DOI
10.1074/jbc.M304474200 · DOI · Paper page
10.1016/j.bbamcr.2004.09.024 · DOI · Paper page
10.1074/jbc.M301410200 · DOI
10.1074/jbc.C100008200 · DOI · Paper page
10.1111/j.1600-0854.2011.01305.x · DOI
10.1016/0014-5793(95)01450-0 · DOI
10.1016/S0166-2236(02)00013-9 · DOI
10.1074/jbc.M113.470500 · DOI
10.1126/science.1230161 · DOI · Paper page
10.1111/j.1600-0854.2008.00766.x · DOI
10.1091/mbc.E10-11-0874 · DOI
10.1038/ncb3054 · DOI · Paper page
10.1111/j.1600-0854.2007.00679.x · DOI
10.1128/MCB.00595-08 · DOI
10.1146/annurev.cb.07.110191.000325 · DOI · Paper page
10.1172/JCI39678 · DOI · Paper page
10.1038/srep24045 · DOI
10.1182/blood-2010-07-295287 · DOI
10.1101/gr.2659105 · DOI · Paper page
10.1096/fj.02-0497fje · DOI
10.1074/jbc.M402820200 · DOI
10.1038/nn.2715 · DOI · Paper page
10.1038/ncb758 · DOI · Paper page
10.1093/jb/mvj012 · DOI
10.1038/ncomms7780 · DOI
10.1016/j.immuni.2005.12.002 · DOI
10.1074/jbc.271.18.10946 · DOI · Paper page
10.1007/s10534-012-9522-1 · DOI
10.1016/j.neuropharm.2013.04.035 · DOI
10.1111/j.1600-0854.2009.00948.x · DOI
10.1078/0171-9335-00374 · DOI
10.1073/pnas.1431613100 · DOI · Paper page
10.1152/physrev.00027.2001 · DOI · Paper page
10.1083/jcb.201307100 · DOI
10.1016/j.gene.2014.11.051 · DOI · Paper page
10.3389/fnmol.2016.00004 · DOI · Paper page
10.1074/jbc.273.45.30012 · DOI · Paper page
10.1074/jbc.M111.225615 · DOI
10.1038/ncb983 · DOI · Paper page
10.1038/embor.2012.187 · DOI
10.1128/JVI.00591-14 · DOI
10.1242/jcs.033951 · DOI · Paper page
10.1038/srep06992 · DOI
Harding C, 1984, Eur J Cell Biol, 35, 256
10.1016/S0960-9822(99)80091-8 · DOI · Paper page
10.1073/pnas.250277297 · DOI · Paper page
10.1074/jbc.C000906200 · DOI
10.1074/jbc.M110443200 · DOI
10.1042/BJ20041241 · DOI · Paper page
10.1091/mbc.E07-12-1219 · DOI
10.1083/jcb.153.4.649 · DOI · Paper page
10.1016/j.devcel.2011.05.015 · DOI · Paper page
10.1016/j.devcel.2012.08.003 · DOI
10.1016/j.heares.2004.01.005 · DOI
10.1146/annurev.biochem.67.1.425 · DOI · Paper page
10.1038/sj.emboj.7600137 · DOI
10.1146/annurev.cellbio.19.110701.154617 · DOI · Paper page
10.1016/S0092-8674(00)80982-4 · DOI · Paper page
10.1182/blood-2002-08-2543 · DOI · Paper page
Hideshima T, 2001, Cancer Res, 61, 3071
10.1083/jcb.149.1.67 · DOI · Paper page
10.1038/nn.2644 · DOI · Paper page
10.1016/j.febslet.2006.11.075 · DOI
10.1186/1741-7007-8-72 · DOI
10.1073/pnas.0904880106 · DOI
10.1101/gad.11.20.2701 · DOI · Paper page
10.1073/pnas.0707416104 · DOI · Paper page
10.1111/j.1600-065X.2008.00655.x · DOI
10.1016/j.molcel.2006.02.018 · DOI · Paper page
10.1073/pnas.92.7.2563 · DOI · Paper page
10.1146/annurev-biophys-042910-155404 · DOI
10.1111/j.1365-2990.1993.tb00418.x · DOI
10.1016/S1534-5807(02)00409-4 · DOI · Paper page
10.4049/jimmunol.0901521 · DOI
10.1371/journal.pone.0039582 · DOI
10.1074/jbc.M108552200 · DOI
10.1128/MCB.17.11.6236 · DOI
10.1113/JP270043 · DOI
10.1091/mbc.E02-08-0532 · DOI · Paper page
10.1038/ncb2257 · DOI · Paper page
10.1074/jbc.M705580200 · DOI
10.1096/fj.00-0191com · DOI · Paper page
10.1046/j.1523-1755.2001.060002466.x · DOI
10.1016/j.ceb.2013.11.005 · DOI · Paper page
10.1042/BJ20141282 · DOI
10.1016/j.tins.2010.02.004 · DOI
10.1074/jbc.M007251200 · DOI · Paper page
10.1034/j.1600-0854.2002.31006.x · DOI
10.1016/S0092-8674(01)00434-2 · DOI · Paper page
10.1038/nrm973 · DOI · Paper page
10.1016/S1097-2765(00)00134-9 · DOI · Paper page
10.1371/journal.pone.0053509 · DOI
10.1016/bs.pmbts.2015.02.005 · DOI
10.1016/j.neuron.2013.02.029 · DOI · Paper page
10.1016/j.molcel.2011.08.025 · DOI · Paper page
10.1091/mbc.E06-09-0861 · DOI
10.1111/gtc.12103 · DOI
10.1038/33416 · DOI · Paper page
10.1152/ajprenal.00441.2009 · DOI
10.1002/j.1460-2075.1994.tb06627.x · DOI · Paper page
10.1038/nrm2731 · DOI · Paper page
10.1074/jbc.M203018200 · DOI
10.1242/dev.01922 · DOI · Paper page
10.1182/blood-2012-10-459883 · DOI · Paper page
10.1074/jbc.M706974200 · DOI
10.1038/nature13392 · DOI · Paper page
10.1074/jbc.M512215200 · DOI
10.1073/pnas.1302792110 · DOI
10.1172/JCI68996 · DOI
10.1021/acs.jmedchem.5b00054 · DOI · Paper page
10.1016/S1534-5807(01)00092-2 · DOI · Paper page
10.1242/dev.01825 · DOI · Paper page
10.1073/pnas.86.4.1168 · DOI · Paper page
Langdon WY, 1989, J Virol, 63, 5420, 10.1128/JVI.63.12.5420-5424.1989 · DOI
10.1371/journal.pbio.0030096 · DOI · Paper page
10.1093/emboj/18.13.3616 · DOI · Paper page
10.1016/j.cell.2010.06.011 · DOI · Paper page
10.1016/S1097-2765(00)80231-2 · DOI · Paper page
10.1210/en.2005-1313 · DOI
10.1371/journal.pbio.1001239 · DOI
10.1371/journal.pgen.1006062 · DOI
10.1038/onc.2009.162 · DOI
10.1128/JVI.77.3.1812-1819.2003 · DOI · Paper page
10.1111/j.1471-4159.2011.07221.x · DOI · Paper page
10.1073/pnas.96.11.6273 · DOI · Paper page
10.1182/blood-2007-08-110445 · DOI
10.1128/MCB.22.11.3599-3609.2002 · DOI · Paper page
10.2353/ajpath.2009.080861 · DOI
10.1074/jbc.M606643200 · doi:10.1074/jbc.m606643200
10.1158/1078-0432.CCR-13-2490 · DOI
10.1007/128_2011_157 · DOI
10.1042/BJ20120662 · DOI
10.1073/pnas.1217477109 · DOI
10.1523/JNEUROSCI.5944-10.2011 · DOI
10.2217/pgs.11.178 · doi:10.2217/pgs.11.178
10.1038/embor.2012.18 · DOI
10.1146/annurev-biochem-060210-093619 · DOI · Paper page

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Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 772
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Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Regulation of reactive oxygen species during plant immunity through phosphorylation and ubiquitination of RBOHD
Lee, D., Lal, N. K., Lin, Z.-J. D., Ma, S., Liu, J., Castro, B., Toruño, T., Dinesh-Kumar, S. P., & Coaker, G. (2020) · Nature Communications · doi:10.1038/s41467-020-15601-5 · Cited by 319
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Chen, J., Qiu, S., Li, W., Wang, K., Zhang, Y., Yang, H., Liu, B., Li, G., Li, L., Chen, M., et al. (2023) · Cell Research · doi:10.1038/s41422-023-00789-0 · Cited by 195
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Authors: Foot, N., Henshall, T., & Kumar, S.
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 2017-01
Volume: 97
Issue: 1
Pages: 253-281
ISSN: 0031-9333 (ISSN-L)
1522-1210
DOI: 10.1152/physrev.00012.2016
OpenAlex: W2560345632
Cited by: 262
References: 25
FWCI: 1.12
Type: journal article
Language: en
Open access: closed
Funders: Department of Health, Australian Government | National Health and Medical Research Council (NHMRC) (1059393, 1099307, 1103006)

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Ubiquitination and the Regulation of Membrane Proteins

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