The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
Abstract
Rab GTPases control vesicle movement and tethering membrane events in membrane trafficking. We used the 38 human Rab GTPase activating proteins (GAPs) to identify which of the 60 Rabs encoded in the human genome function at the Golgi complex. Surprisingly, this screen identified only two GAPs, RN-tre and TBC1D20, disrupting both Golgi organization and protein transport. RN-tre is the GAP for Rab43, and controls retrograde transport into the Golgi from the endocytic pathway. TBC1D20 is the ER-localized GAP for Rab1, and is the only GAP blocking the delivery of secretory cargo from the ER to the cell surface. Strikingly, its expression causes the loss of the Golgi complex, highlighting the importance of Rab1 for Golgi biogenesis. These effects can be antagonized by reticulon, a binding partner for TBC1D20 in the ER. Together, these findings indicate that Rab1 and Rab43 are key Rabs required for the biogenesis and maintenance of a functional Golgi structure, and suggest that other Rabs acting at the Golgi complex are likely to be functionally redundant.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Loss of RAB1A/B impaired secretion (Fig. 6d,e), serving as a positive control3637.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [36]
Citations
Cites
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
The Mechanisms of Vesicle Budding and Fusion
Bonifacino, J. S., & Glick, B. S. (2004) · Cell · doi:10.1016/s0092-8674(03)01079-1 · Cited by 1,908
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models
Cooper, A. A., Gitler, A. D., Cashikar, A. G., Haynes, C. M., Hill, K. J., Bhullar, B., Liu, K., Xu, K., Strathearn, K. E., Liu, F., et al. (2006) · Science · doi:10.1126/science.1129462 · Cited by 1,411
A Class of Membrane Proteins Shaping the Tubular Endoplasmic Reticulum
Voeltz, G. K., Prinz, W. A., Shibata, Y., Rist, J. M., & Rapoport, T. A. (2006) · Cell · doi:10.1016/j.cell.2005.11.047 · Cited by 1,133
Tisdale, E. J., Bourne, J. R., Khosravi-Far, R., Der, C. J., & Balch, W. E. (1992) · The Journal of cell biology · doi:10.1083/jcb.119.4.749 · Cited by 500
Targeting Rab GTPases to distinct membrane compartments
Pfeffer, S. R., & Aivazian, D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1500 · Cited by 462
Transport-vesicle targeting: tethers before SNAREs
Pfeffer, S. R. (1999) · Nature Cell Biology · doi:10.1038/8967 · Cited by 449
The organization of endoplasmic reticulum export complexes.
Bannykh, S. I., Rowe, T., & Balch, W. E. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.1.19 · Cited by 440
Procollagen Traverses the Golgi Stack without Leaving the Lumen of Cisternae
Bonfanti, L., Aa, M., Martínez‐Menárguez, J. A., Martella, O., Fusella, A., Baldassarre, M., Buccione, R., Geuze, H. J., Mirоnоv, A. A., & Luini, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81723-7 · Cited by 419
Flagged first, then by citations
Cited by
Sorted by citations
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
ARF family G proteins and their regulators: roles in membrane transport, development and disease
Donaldson, J. G., & Jackson, C. L. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3117 · Cited by 914
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586
Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic
Sakamoto, K., & Holman, G. D. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90331.2008 · Cited by 481
Barr, F. A., & Lambright, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.007 · Cited by 433
Self-citationThe Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b
Müller, M. P., Peters, H., Blümer, J., Blankenfeldt, W., Goody, R. S., & Itzen, A. (2010) · Science · doi:10.1126/science.1192276 · Cited by 344
Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
Yoshimura, S.-I., Gerondopoulos, A., Linford, A., Rigden, D. J., & Barr, F. A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008051 · Cited by 317
Self-citationEarly endosomes and endosomal coatomer are required for autophagy
Razi, M., Chan, E. Y. W., & Tooze, S. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810098 · Cited by 298
Lopes, K. D. P., Snijders, G. J. L., Humphrey, J., Allan, A., Sneeboer, M. A. M., Navarro, E., Schilder, B. M., Vialle, R. A., Parks, M., Missall, R., et al. (2022) · Nature Genetics · doi:10.1038/s41588-021-00976-y · Cited by 273
Lipid droplet-organelle interactions; sharing the fats
Murphy, S., Martin, S., & Parton, R. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.07.004 · Cited by 265
Rab GTPases and membrane identity: Causal or inconsequential?
Barr, F. A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201306010 · Cited by 247
Self-citationThe reticulons: a family of proteins with diverse functions
Yang, Y. S., & Strittmatter, S. M. (2007) · Genome biology · doi:10.1186/gb-2007-8-12-234 · Cited by 211
TBC proteins: GAPs for mammalian small GTPase Rab?
Fukuda, M. (2011) · Bioscience Reports · doi:10.1042/bsr20100112 · Cited by 207
Thousands of Rab GTPases for the Cell Biologist
Diekmann, Y., Seixas, E., Gouw, M., Tavares-Cadete, F., Seabra, M. C., & Pereira‐Leal, J. B. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002217 · Cited by 193
Illuminating the functional and structural repertoire of human TBC/RABGAPs
Frasa, M. A. M., Koessmeier, K. T., Ahmadian, M. R., & Braga, V. M. M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3267 · Cited by 191
Loss-of-Function Mutations in RAB18 Cause Warburg Micro Syndrome
Bem, D., Yoshimura, S., Bastos, R. N., Bond, F. F., Kurian, M. A., Rahman, F., Handley, M. T., Hadzhiev, Y., Masood, I., Straatman-Iwanowska, A. A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.03.012 · Cited by 174
Self-citationA Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway
Rivera-Molina, F. E., & Novick, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906536106 · Cited by 170
TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic
Lamb, C. A., Nühlen, S., Judith, D., Frith, D., Snijders, A. P., Behrends, C., & Tooze, S. A. (2015) · The EMBO Journal · doi:10.15252/embj.201592695 · Cited by 176
Rab18 and Rab43 have key roles in ER-Golgi trafficking
Dejgaard, S. Y., Murshid, A., Erman, A., Mancini, Ö. K., Verbich, D., Lodge, R., Dejgaard, K., Ly-Hartig, T. B. N., Pepperkok, R., Simpson, J. C., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.021808 · Cited by 167
Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER
Hughes, H., Budnik, A., Schmidt, K., Palmer, K. J., Mantell, J., Noakes, C., Johnson, A., Carter, D. A., Verkade, P., Watson, P., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.044032 · Cited by 160
Self-citationAutophagy: a multifaceted player in the fate of sperm
Wang, M., Zeng, L., Su, P., Ma, L., Zhang, M., & Zhang, Y. (2021) · Human Reproduction Update · doi:10.1093/humupd/dmab043 · Cited by 155
Sun, T., Wang, X., He, H. H., Sweeney, C. J., Liu, S. X., Brown, M. A., Balk, S. P., Lee, G.-S., & Kantoff, P. W. (2013) · Oncogene · doi:10.1038/onc.2013.230 · Cited by 146
Rab18 and a Rab18 GEF complex are required for normal ER structure
Gerondopoulos, A., Bastos, R. N., Yoshimura, S., Anderson, R. L., Carpanini, S. M., Aligianis, I. A., Handley, M. T., & Barr, F. A. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201403026 · Cited by 144
Self-citationBioanalysis of Eukaryotic Organelles
Satori, C. P., Henderson, M. M., Krautkramer, E. A., Košťál, V., Distefano, M. M., & Arriaga, E. A. (2013) · Chemical Reviews · doi:10.1021/cr300354g · Cited by 147
Liegel, R. P., Handley, M. T., Ronchetti, A., Brown, S. D. M., Langemeyer, L., Linford, A., Chang, B., Morris-Rosendahl, D. J., Carpanini, S. M., Posmyk, R., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.10.011 · Cited by 140
Self-citationStructural Mechanisms for Regulation of Membrane Traffic by Rab GTPases
Lee, M. G., Mishra, A. K., & Lambright, D. G. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00942.x · Cited by 142
PITPNC1 Recruits RAB1B to the Golgi Network to Drive Malignant Secretion
Halberg, N., Sengelaub, C. A., Navrazhina, K., Molina, H., Uryu, K., & Tavazoie, S. F. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.02.013 · Cited by 137
Function and Regulation of the Endosomal Fusion and Fission MachineriesPreprint
Gautreau, A. M., Oguievetskaia, K., & Ungermann, C. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016832 · Cited by 129
Shaping the Endoplasmic Reticulum into a Social Network
Zhang, H., & Hu, J. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.06.002 · Cited by 126
TBC1D20 Is a Rab1 GTPase-activating Protein That Mediates Hepatitis C Virus Replication
Sklan, E. H., Serrano, R., Einav, S., Pfeffer, S. R., Lambright, D. G., & Glenn, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705221200 · Cited by 126
Assembly, organization, and function of the COPII coat
Hughes, H., & Stephens, D. J. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0363-x · Cited by 121
Self-citationSoo, K. Y., Halloran, M. A., Sundaramoorthy, V., Parakh, S., Toth, R. P., Southam, K. A., McLean, C., Lock, P., King, A. E., Farg, M. A., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1468-2 · Cited by 125
mTrs130 Is a Component of a Mammalian TRAPPII Complex, a Rab1 GEF That Binds to COPI-coated Vesicles
Yamasaki, A., Menon, S., Yu, S. S. B., Barrowman, J., Meerloo, T., Oorschot, V. M. J., Klumperman, J., Satoh, A., & Ferro‐Novick, S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-05-0387 · Cited by 115
Are Rab proteins the link between Golgi organization and membrane trafficking?
Liu, S., & Storrie, B. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1021-6 · Cited by 117
Rab proteins as major determinants of the Golgi complex structure
Goud, B., Liu, S., & Storrie, B. (2017) · Small GTPases · doi:10.1080/21541248.2017.1384087 · Cited by 107
Wendler, F., Gillingham, A. K., Sinka, R., Rosa-Ferreira, C., Gordon, D. E., Franch‐Marro, X., Peden, A. A., Vincent, J., & Munro, S. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.350 · Cited by 106
Transport to Late Endosomes Is Required for Efficient Reovirus Infection
Mainou, B. A., & Dermody, T. S. (2012) · Journal of Virology · doi:10.1128/jvi.00100-12 · Cited by 104
Recent Advances in Understanding Amino Acid Sensing Mechanisms that Regulate mTORC1
Zheng, L., Zhang, W., Zhou, Y., Li, F., Wei, H., & Peng, J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17101636 · Cited by 109
Rab Proteins and the Secretory Pathway: The Case of Rab18 in Neuroendocrine Cells
Vázquez‐Martínez, R., & Malagón, M. M. (2011) · Frontiers in Endocrinology · doi:10.3389/fendo.2011.00001 · Cited by 98
Bacterial Pathogens Commandeer Rab GTPases to Establish Intracellular Niches
Stein, M., Müller, M. P., & Wandinger‐Ness, A. (2012) · Traffic · doi:10.1111/tra.12000 · Cited by 93
Hayes, G. L., Brown, F. C., Haas, A. K., Nottingham, R. M., Barr, F. A., & Pfeffer, S. R. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0740 · Cited by 92
Self-citationReticulon 4B (Nogo-B) is necessary for macrophage infiltration and tissue repair
Yu, J., Fernandez-Hernando, C. F., Suárez, Y., Schleicher, M., Hao, Z., Wright, P. L., Lorenzo, A. D., Kyriakides, T. R., & Sessa, W. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907359106 · Cited by 91
The parasite Toxoplasma sequesters diverse Rab host vesicles within an intravacuolar network
Romano, J. D., Nolan, S. J., Porter, C. M., Ehrenman, K., Hartman, E. J., Hsia, R., & Coppens, I. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701108 · Cited by 88
Rab33b and Rab6 are Functionally Overlapping Regulators of Golgi Homeostasis and Trafficking
Starr, T., Sun, Y., Wilkins, N., & Storrie, B. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01051.x · Cited by 89
Role of vesicle tethering factors in the ER–Golgi membrane traffic
Sztul, E. S., & Lupashin, V. V. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.083 · Cited by 85
Miller, V. J., Sharma, P., Kudlyk, T. A., Frost, L., Rofe, A. P., Watson, I. J., Duden, R., Lowe, M., Lupashin, V. V., & Ungár, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.426767 · Cited by 84
Protein LidA from Legionella is a Rab GTPase supereffector
Schoebel, S., Cichy, A., Goody, R. S., & Itzen, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113133108 · Cited by 79
Avanzato, D., Pupo, E., Ducano, N., Isella, C., Bertalot, G., Luise, C., Pece, S., Bruna, A., Rueda, O. M., Caldas, C., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3018 · Cited by 82
RAB43 facilitates cross-presentation of cell-associated antigens by CD8α+ dendritic cells
Kretzer, N. M., Theisen, D. J., Tussiwand, R., Briseño, C. G., Grajales‐Reyes, G. E., Wu, X., Durai, V., Albring, J. C., Bagadia, P., Murphy, T. L., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160597 · Cited by 84
Zenner, H. L., Yoshimura, S., Barr, F. A., & Crump, C. M. (2011) · Journal of Virology · doi:10.1128/jvi.00500-11 · Cited by 76
Self-citationGolgi fragmentation is Rab and SNARE dependent in cellular models of Parkinson’s disease
Rendón, W. O., Martínez‐Alonso, E., Tomás, M., Martínez-Martínez, N., & Martínez‐Menárguez, J. A. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-1059-4 · Cited by 79
TBC1D20 mediates autophagy as a key regulator of autophagosome maturation
Sidjanin, D. J., Park, A. K., Ronchetti, A., Martins, J., & Jackson, W. T. (2016) · Autophagy · doi:10.1080/15548627.2016.1199300 · Cited by 79
The Rab family of proteins: 25 years on
Kelly, E. E., Horgan, C. P., Goud, B., & McCaffrey, M. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120203 · Cited by 72
Defects in the COG complex and COG-related trafficking regulators affect neuronal Golgi function
Climer, L. K., Dobretsov, M. G., & Lupashin, V. V. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00405 · Cited by 71
Marie, M., Dale, H. A., Sannerud, R., & Saraste, J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1229 · Cited by 69
Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases
Ishida, M., Oguchi, M. E., & Fukuda, M. (2016) · Cell Structure and Function · doi:10.1247/csf.16008 · Cited by 68
Consequences of Rab GTPase dysfunction in genetic or acquired human diseases
Banworth, M. J., & Li, G. (2017) · Small GTPases · doi:10.1080/21541248.2017.1397833 · Cited by 68
Intermediate compartment (IC): from pre-Golgi vacuoles to a semi-autonomous membrane system
Saraste, J., & Marie, M. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1717-2 · Cited by 69
Aizawa, M., & Fukuda, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.669242 · Cited by 68
Langemeyer, L., Bastos, R. N., Cai, Y., Itzen, A., Reinisch, K. M., & Barr, F. A. (2014) · eLife · doi:10.7554/elife.01623 · Cited by 66
Self-citationCatalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail
Gavriljuk, K., Gazdag, E. M., Itzen, A., Kötting, C., Goody, R. S., & Gerwert, K. B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214431110 · Cited by 68
Greninger, A. L., Knudsen, G. M., Betegon, M., Burlingame, A. L., & DeRisi, J. L. (2013) · mBio · doi:10.1128/mbio.00098-13 · Cited by 65
Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB
Gazdag, E. M., Streller, A., Haneburger, I., Hilbi, H., Vetter, I. R., Goody, R. S., & Itzen, A. (2013) · EMBO Reports · doi:10.1038/embor.2012.211 · Cited by 64
Uptake of oomycete RXLR effectors into host cells by clathrin-mediated endocytosis
Wang, H., Wang, S., Wang, W., Xu, L., Welsh, L. R. J., Gierliński, M., Whisson, S. C., Hemsley, P. A., Boevink, P. C., & Birch, P. R. J. (2023) · The Plant Cell · doi:10.1093/plcell/koad069 · Cited by 64
RUTBC1 Protein, a Rab9A Effector That Activates GTP Hydrolysis by Rab32 and Rab33B Proteins
Nottingham, R. M., Ganley, I. G., Barr, F. A., Lambright, D. G., & Pfeffer, S. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261115 · Cited by 62
Self-citationEvolution of Tre-2/Bub2/Cdc16 (TBC) Rab GTPase-activating proteins
Gabernet‐Castello, C., O’Reilly, A., Dacks, J. B., & Field, M. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-07-0557 · Cited by 57
Rab proteins of the endoplasmic reticulum: functions and interactors
Sandoval, C. O., & Simmen, T. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120158 · Cited by 58
Nevo-Yassaf, I., Yaffe, Y., Asher, M., Ravid, O., Eizenberg, S., Henis, Y. I., Nahmias, Y., Hirschberg, K., & Sklan, E. H. (2012) · Journal of Virology · doi:10.1128/jvi.00496-12 · Cited by 56
Warburg Micro syndrome is caused by RAB18 deficiency or dysregulation
Handley, M. T., Carpanini, S. M., Mali, G. R., Sidjanin, D. J., Aligianis, I. A., Jackson, I. J., & FitzPatrick, D. R. (2015) · Open Biology · doi:10.1098/rsob.150047 · Cited by 55
AMPylation Is Critical for Rab1 Localization to Vacuoles Containing Legionella pneumophila
Hardiman, C. A., & Roy, C. R. (2014) · mBio · doi:10.1128/mbio.01035-13 · Cited by 55
Autophagy: A Double-Edged Sword in Male Reproduction
Yan, Q., Zhang, Y., Wang, Q., & Yuan, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315273 · Cited by 56
The GTPase-Activating Protein RN-tre Controls Focal Adhesion Turnover and Cell Migration
Palamidessi, A., Frittoli, E., Ducano, N., Offenhäuser, N., Sigismund, S., Kajiho, H., Parazzoli, D., Oldani, A., Gobbi, M., Serini, G., et al. (2013) · Current Biology · doi:10.1016/j.cub.2013.09.060 · Cited by 56
The GTPase Rab43 Controls the Anterograde ER-Golgi Trafficking and Sorting of GPCRs
Li, C., Wei, Z., Fan, Y., Huang, W. Y., Su, Y., Li, H., Dong, Z., Fukuda, M., Khater, M., & Wu, G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.011 · Cited by 54
Cheng, W., Yin, K., Lu, D., Li, B., Zhu, D., Chen, Y., Zhang, H., Xu, S., Chai, J., & Gu, L. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002528 · Cited by 52
Ishibashi, K., Kanno, E., Itoh, T., & Fukuda, M. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01251.x · Cited by 52
The Msb3/Gyp3 GAP controls the activity of the Rab GTPases Vps21 and Ypt7 at endosomes and vacuoles
Lachmann, J., Barr, F. A., & Ungermann, C. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1030 · Cited by 52
Self-citationOgawa, M., Matsuda, R., Takada, N., Tomokiyo, M., Yamamoto, S., Shizukuishi, S., Yamaji, T., Yoshikawa, Y., Yoshida, M., Tanida, I., et al. (2018) · Cellular Microbiology · doi:10.1111/cmi.12846 · Cited by 52
Ypt/Rab GTPases: Principles learned from yeast
Lipatova, Z., Hain, A. U. P., Nazarko, V. Y., & Segev, N. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1014023 · Cited by 51
How Rab Proteins Determine Golgi Structure
Liu, S., & Storrie, B. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2014.12.002 · Cited by 54
Golgi trafficking defects in postnatal microcephaly: The evidence for “Golgipathies”
Passemard, S., Perez, F., Colin, E., Rasika, S., Gressèns, P., & Ghouzzi, V. E. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.007 · Cited by 50
Tau secretion is correlated to an increase of Golgi dynamics
Mohamed, N., Desjardins, A., & Leclerc, N. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178288 · Cited by 55
Rab25 GTPase: Functional roles in cancer
Wang, S., Hu, C., Wu, F., & He, S. (2017) · Oncotarget · doi:10.18632/oncotarget.19571 · Cited by 61
Ishida, M., Ohbayashi, N., Maruta, Y., Ebata, Y., & Fukuda, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.109314 · Cited by 49
Rab30 is required for the morphological integrity of the Golgi apparatus
Kelly, E. E., Giordano, F., Horgan, C. P., Jollivet, F., Raposo, G., & McCaffrey, M. (2011) · Biology of the Cell · doi:10.1111/boc.201100080 · Cited by 50
Thomas, C., Rousset, R., & Noselli, S. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2009.05.001 · Cited by 49
Khan, N. Z., Lindquist, E., & Aronsson, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059898 · Cited by 54
Spatial and Functional Aspects of ER-Golgi Rabs and Tethers
Saraste, J. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00028 · Cited by 49
Goueli, B. S., Powell, M. B., Finger, E. C., & Pfeffer, S. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204540109 · Cited by 41
TBC1D13 is a RAB35 Specific GAP that Plays an Important Role in GLUT4 Trafficking in Adipocytes
Davey, J. R., Humphrey, S. J., Junutula, J. R., Mishra, A. K., Lambright, D. G., James, D. E., & Stöckli, J. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01397.x · Cited by 53
Carpanini, S. M., McKie, L., Thomson, D., Wright, A. K., Gordon, S. L., Roche, S. L., Handley, M. T., Morrison, H., Brownstein, D. G., Wishart, T. M., et al. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.015222 · Cited by 46
Specific TBC Domain-Containing Proteins Control the ER-Golgi-Plasma Membrane Trafficking of GPCRs
Wei, Z., Zhang, M., Li, C., Huang, W. Y., Fan, Y., Guo, J., Khater, M., Fukuda, M., Dong, Z., Hu, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.033 · Cited by 46
Flowerdew, S. E., & Burgoyne, R. D. (2009) · Biochemical Journal · doi:10.1042/bj20081736 · Cited by 48
Functions of reticulons in plants: What we can learn from animals and yeasts
Nziengui, H., & Schoefs, B. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8373-y · Cited by 44
GTRAP3‐18 serves as a negative regulator of Rab1 in protein transport and neuronal differentiation
Maier, S., Reiterer, V., Ruggiero, A. M., Rothstein, J. D., Thomas, S., Dahm, R., Sitte, H. H., & Farhan, H. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00303.x · Cited by 42
Rab18: new insights into the function of an essential protein
Dejgaard, S. Y., & Presley, J. F. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03050-3 · Cited by 42
Rab GTPase function in Golgi trafficking
Barr, F. A. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.03.007 · Cited by 40
Self-citationRegulation of RabGAPs involved in insulin action
Mafakheri, S., Chadt, A., & Al‐Hasani, H. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170479 · Cited by 39
Modulation of Small GTPases by Legionella
Goody, R. S., & Itzen, A. (2013) · Current topics in microbiology and immunology · doi:10.1007/82_2013_340 · Cited by 38
Retrograde vesicle transport in the Golgi
Cottam, N. P., & Ungár, D. (2011) · PROTOPLASMA · doi:10.1007/s00709-011-0361-7 · Cited by 36
Preadipocyte factor 1 induces pancreatic ductal cell differentiation into insulin-producing cells
Rhee, M., Lee, S., Kim, J.-W., Ham, D., Park, H., Yang, H. K., Shin, J., Cho, J., Kim, Y., Youn, B., et al. (2016) · Scientific Reports · doi:10.1038/srep23960 · Cited by 38
Metadata
- Authors
- Haas, A. K., Yoshimura, S.-I., Stephens, D. J., Preisinger, C., Fuchs, E., & Barr, F. A.
- Affiliations
- University of Liverpool (GB)
- University of Bristol (GB)
- Max Planck Institute of Biochemistry (DE)
- Corresponding author
- Barr, Francis A.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2007-09-01
- Volume
- 120
- Issue
- 17
- Pages
- 2997-3010
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2064782801
- Cited by
- 201
- References
- 56
- Citations by year
- 2025: 8 · 2024: 5 · 2023: 8 · 2022: 7 · 2021: 11 · 2020: 8 · 2019: 10 · 2018: 9 · 2017: 10 · 2016: 16 · 2015: 9 · 2014: 13 · 2013: 15 · 2012: 21
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Explore Bristol Research (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Bristol Research (University of Bristol) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- Rab GTPases, Rab1, Rab GTPase-activating protein, reticulons, retrograde transport, secretory pathway, ER-Golgi transport, membrane trafficking, functional redundancy
- MeSH terms
- rab11 GTP-Binding Proteins, Animals, Biological Transport, Endoplasmic Reticulum, Golgi Apparatus, HeLa Cells, Humans, Nerve Tissue Proteins, Phenotype, Recombinant Fusion Proteins, Genome, Human, rab GTP-Binding Proteins, rab1 GTP-Binding Proteins, Two-Hybrid System Techniques, RNA Interference
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 ›
Are you an author, or do you see a problem with this page? Request a review