Role of Rab GTPases in Membrane Traffic and Cell Physiology

Hutagalung, Alex H.; Novick, Peter J.

doi:10.1152/physrev.00059.2009

Cited by 1,460

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Role of Rab GTPases in Membrane Traffic and Cell Physiology

Hutagalung, Alex H., Novick, Peter J.·2011·Physiological Reviews

DOI 10.1152/physrev.00059.2009PMC PMC3710122

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Abstract

Intracellular membrane traffic defines a complex network of pathways that connects many of the membrane-bound organelles of eukaryotic cells. Although each pathway is governed by its own set of factors, they all contain Rab GTPases that serve as master regulators. In this review, we discuss how Rabs can regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. Some of the many regulatory functions performed by Rabs include interacting with diverse effector proteins that select cargo, promoting vesicle movement, and verifying the correct site of fusion. We describe cascade mechanisms that may define directionality in traffic and ensure that different Rabs do not overlap in the pathways that they regulate. Throughout this review we highlight how Rab dysfunction leads to a variety of disease states ranging from infectious diseases to cancer.

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RAB10 is involved in membrane trafficking regulation and moving proteins from the Golgi apparatus to the membrane.
“is involved in membrane trafficking regulation and moving proteins from the Golgi apparatus to the membrane [58, 59]”
From Linkage, whole genome sequence, and biological data implicate variants in RAB10 in Alzheimer’s disease resilience (2017) · cites this paper as [58]
The References (no page available) include a study titled “Rab10 regulates membrane transport through early endosomes,” supporting RAB10’s role in membrane trafficking. The cited paper passages do not establish that RAB10 moves proteins from the Golgi to the plasma membrane; the adjacent reference describes that route without attributing it to RAB10. (LLM, conf=0.78)
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The Rab5 effector EEA1 is a core component of endosome docking
Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854
Activation of endosomal dynein motors by stepwise assembly of Rab7–RILP–p150Glued, ORP1L, and the receptor βlll spectrin
Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505
New Component of the Vacuolar Class C-Vps Complex Couples Nucleotide Exchange on the Ypt7 Gtpase to Snare-Dependent Docking and Fusion
Wurmser, A. E., Sato, T. K., & Emr, S. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.3.551 · Cited by 425
RAB23 Mutations in Carpenter Syndrome Imply an Unexpected Role for Hedgehog Signaling in Cranial-Suture Development and Obesity
Jenkins, D., Seelow, D., Jehee, F. S., Perlyn, C. A., Alonso, L. G., Bueno, D. F., Donnai, D., Josifiova, D., Mathijssen, I. M. J., Morton, J. E. V., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/518047 · Cited by 276
Rab27a
Bahadoran, P., Aberdam, E., Mantoux, F., Buscà, R., Bille, K., Yalman, N., de Saint-Basile, G., Casaroli-Marano, R., Ortonne, J.-P., & Ballotti, R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.843 · Cited by 221
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Flagged first, then by citations

Research works printed but not linked: 490

10.1083/jcb.200510010 · DOI
10.1002/j.1460-2075.1994.tb06860.x · DOI
10.1042/BST0330652 · DOI
10.1038/ng1517 · DOI
10.1086/502681 · DOI
10.1126/science.289.5478.444 · DOI · Paper page
10.1091/E03-04-0227 · DOI
10.1083/jcb.200204081 · DOI
10.1016/j.humpath.2005.10.017 · DOI
10.1016/j.jmb.2009.04.062 · DOI
10.1016/S0969-2126(03)00034-0 · DOI
10.1074/jbc.M105833200 · DOI
10.1074/jbc.M308740200 · DOI
10.1016/0092-8674(93)90639-8 · DOI
10.1083/jcb.200307046 · DOI
10.1083/jcb.200408165 · DOI
10.1016/j.cub.2008.06.028 · DOI
10.1091/mbc.E05-08-0799 · DOI · Paper page
10.1083/jcb.109.3.1015 · DOI
10.1111/j.1600-0854.2008.00827.x · DOI
10.1073/pnas.83.23.9075 · DOI
10.1083/jcb.107.4.1369 · DOI
10.1111/j.1469-1809.2007.00412.x · DOI
10.1016/S0960-9822(99)80167-5 · DOI
10.1093/emboj/17.12.3258 · DOI
10.1186/1471-2121-6-15 · DOI · Paper page
10.1074/jbc.M503925200 · DOI
10.1074/jbc.M109.046102 · DOI
10.1002/j.1460-2075.1996.tb01037.x · DOI
10.1111/j.1600-0854.2007.00585.x · DOI
10.1006/bbrc.2001.4468 · DOI
10.1002/humu.21086 · DOI
10.1091/mbc.E04-01-0053 · DOI
10.1196/annals.1315.018 · DOI
10.1016/j.ceb.2008.03.009 · DOI · Paper page
10.1038/nrm1985 · DOI
10.1016/j.cell.2007.05.018 · DOI · Paper page
10.1126/science.1110225 · DOI
10.1038/362560a0 · DOI
10.1083/jcb.200801001 · DOI
10.1128/MCB.15.3.1137 · DOI
10.1128/MMBR.00023-07 · DOI
10.1091/mbc.11.2.467 · DOI
10.1016/j.ejcb.2007.11.003 · DOI · Paper page
10.1242/jcs.018432 · DOI
10.1002/j.1460-2075.1994.tb06892.x · DOI
10.1016/S1040-7952(06)80010-8 · DOI
10.1038/361464a0 · DOI
10.1091/mbc.E08-09-0943 · DOI
10.1016/j.devcel.2007.04.005 · DOI
10.1038/nature05527 · DOI
10.1083/jcb.200505145 · DOI
10.1016/j.cell.2008.04.049 · DOI
10.1046/j.1432-1327.1999.00743.x · DOI
10.1042/bj3380539 · DOI
10.1093/emboj/20.4.683 · DOI · Paper page
10.1111/j.1600-0854.2005.00260.x · DOI
10.1083/jcb.146.2.333 · DOI
10.1126/science.1056791 · DOI
10.1091/mbc.10.1.47 · DOI
10.1111/j.1365-2958.2008.06106.x · DOI
10.1016/j.devcel.2007.08.012 · DOI
10.1074/jbc.M703716200 · DOI
10.1038/353769a0 · DOI
10.1016/0092-8674(90)90369-P · DOI · Paper page
10.1091/mbc.E05-12-1096 · DOI
10.3109/09687680903417470 · DOI · Paper page
10.1074/jbc.M010798200 · DOI
10.1016/S0006-291X(03)00482-0 · DOI
Chen Y, 1996, Eur J Cell Biol, 70, 289
10.1158/0008-5472.CAN-05-0573 · DOI
10.1038/nm1125 · DOI
10.1210/me.2003-0300 · DOI
Chia W, 2009, Biochim Biophys Acta, 1795, 110
10.1038/12075 · DOI · Paper page
10.1016/S1570-9639(03)00236-X · DOI
10.1073/pnas.0702290104 · DOI
10.1016/S1097-2765(03)00445-3 · DOI
10.1091/mbc.E02-10-0654 · DOI
10.1126/science.1129462 · DOI
10.1091/mbc.02-02-0025 · DOI · Paper page
10.1073/pnas.98.4.1637 · DOI
10.1034/j.1600-0854.2003.40205.x · DOI
10.1128/IAI.01020-07 · DOI
10.1016/S0092-8674(01)80013-1 · DOI
10.1016/j.bone.2005.04.021 · DOI
Cremers F, 1994, J Biol Chem, 269, 2111, 10.1016/S0021-9258(17)42142-9 · DOI
10.1073/pnas.122187699 · DOI
10.1038/487 · DOI
10.1093/hmg/11.21.2567 · DOI
10.1093/jnen/63.4.302 · DOI
10.1091/mbc.E03-12-0862 · DOI
10.1046/j.1365-2141.1998.00965.x · DOI
10.1016/j.bbrc.2008.05.060 · DOI
10.1038/ncb744 · DOI
10.1242/jcs.021808 · DOI
10.1111/j.1600-0854.2006.00395.x · DOI
10.1091/mbc.E08-07-0726 · DOI
10.1038/nsmb1232 · DOI
10.1042/bst0240699 · DOI
10.1038/nature05185 · DOI · Paper page
10.1111/j.1600-0854.2005.00299.x · DOI
10.1074/jbc.M708401200 · DOI
10.1083/jcb.200207045 · DOI
10.1016/S0092-8674(00)81171-X · DOI
10.1083/jcb.138.2.283 · DOI
10.1016/0896-6273(95)90346-1 · DOI · Paper page
10.1093/emboj/16.3.465 · DOI
10.1038/nsmb1017 · DOI
10.1016/j.molcel.2007.01.013 · DOI
10.1074/jbc.M401022200 · DOI
10.1016/S0076-6879(01)29070-3 · DOI
10.1038/nature03798 · DOI
10.1126/science.279.5350.580 · DOI
10.1038/35084089 · DOI · Paper page
10.1074/jbc.M109.022582 · DOI
10.1093/emboj/19.24.6713 · DOI
10.1046/j.1600-0854.2003.00141.x · DOI
10.1093/hmg/7.9.1463 · DOI
10.1212/01.wnl.0000265820.51075.61 · DOI
10.1016/j.mib.2007.10.002 · DOI
10.1016/j.bbrc.2004.12.182 · DOI
10.1073/pnas.87.5.1988 · DOI
10.1097/00005072-199603000-00001 · DOI
10.1016/j.bbadis.2008.10.020 · DOI
10.1091/mbc.E03-05-0343 · DOI
10.1186/1471-2121-5-18 · DOI
10.1016/j.cell.2007.12.041 · DOI
10.1083/jcb.200612068 · DOI
10.1074/jbc.M212341200 · DOI
10.1074/jbc.M205765200 · DOI
10.4161/auto.6542 · DOI
10.1074/mcp.M700569-MCP200 · DOI
10.1074/jbc.M306812200 · DOI
10.1074/jbc.M203862200 · DOI
10.1074/jbc.C200005200 · DOI
10.1111/j.1872-034X.2007.00143.x · DOI
10.1111/j.1600-0854.2009.00942.x · DOI
10.1017/S1462399409001148 · DOI
10.1038/11976 · DOI
10.1086/320592 · DOI
10.1038/369493a0 · DOI
10.1038/42954 · DOI
10.1111/j.1460-9568.2008.06310.x · DOI
10.1074/jbc.M404168200 · DOI
10.1038/15658 · DOI
10.1073/pnas.0710685105 · DOI
10.1016/S0079-6123(08)64022-4 · DOI
Goldenring J, 1993, J Biol Chem, 268, 18419, 10.1016/S0021-9258(17)46639-7 · DOI
10.1091/mbc.E02-10-0639 · DOI
10.1007/s00018-005-4486-8 · DOI
10.1016/0092-8674(88)90093-1 · DOI
10.1038/345553a0 · DOI
10.1093/emboj/17.7.1930 · DOI
10.1042/BJ20071094 · DOI
10.1016/j.devcel.2007.06.010 · DOI · Paper page
10.1083/jcb.200510016 · DOI
10.1073/pnas.0601617103 · DOI · Paper page
10.1083/jcb.151.2.439 · DOI
10.1136/jmg.38.6.409 · DOI
10.1242/jcs.00949 · DOI
10.1093/emboj/18.4.1071 · DOI
10.1038/35070029 · DOI
Günther T, 1994, Development, 120, 3119, 10.1242/dev.120.11.3119 · DOI
10.1038/ncb1290 · DOI
10.1016/j.bbrc.2008.10.172 · DOI
10.1046/j.1471-4159.1996.66030889.x · DOI
10.1074/jbc.M104831200 · DOI
10.1074/jbc.M209270200 · DOI
10.1073/pnas.112198799 · DOI
10.1091/mbc.E04-02-0092 · DOI
10.1091/mbc.E02-03-0143 · DOI
10.1016/S0960-9822(00)00864-2 · DOI
10.1042/BSS2007c09 · DOI
10.1091/mbc.E08-07-0740 · DOI · Paper page
10.1074/jbc.M006959200 · DOI
10.1093/hmg/ddn279 · DOI
10.1038/ng.252 · DOI
10.1073/pnas.0605443103 · DOI
10.1091/mbc.E03-03-0160 · DOI
10.1097/SCS.0b013e318184357a · DOI
10.1093/emboj/19.21.5711 · DOI
10.1017/S0033291799002871 · DOI
10.1074/jbc.271.52.33607 · DOI
10.1091/mbc.8.8.1529 · DOI
10.1016/S0092-8674(00)80380-3 · DOI
10.1002/ana.20281 · DOI
10.1016/S0896-6273(00)80493-6 · DOI
10.1083/jcb.123.1.35 · DOI
10.1083/jcb.152.4.795 · DOI
10.1074/jbc.273.25.15734 · DOI
10.1038/sj.emboj.7601274 · DOI
10.1016/j.molcel.2005.04.019 · DOI
10.1016/S0140-6736(04)17104-3 · DOI
10.1074/jbc.M709718200 · DOI
10.1161/01.RES.78.2.343 · DOI
10.1074/jbc.M307260200 · DOI
10.1091/mbc.E07-12-1231 · DOI
10.1128/MCB.22.22.7744-7757.2002 · DOI
10.1038/sj.emboj.7601044 · DOI

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Authors: Hutagalung, A. H., & Novick, P. J.
Affiliations: Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 2011-01
Volume: 91
Issue: 1
Pages: 119-149
ISSN: 0031-9333
1522-1210
DOI: 10.1152/physrev.00059.2009
PMC: PMC3710122
Cited by: 1,460
References: 7
Language: en

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Role of Rab GTPases in Membrane Traffic and Cell Physiology

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