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Lysosome-related organelles: driving post-Golgi compartments into specialisation
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Some cells harbour specialised lysosome-related organelles (LROs) that share features of late endosomes/lysosomes but are functionally, morphologically and/or compositionally distinct. Ubiquitous trafficking machineries cooperate with cell type specific cargoes to produce these organelles. Several genetic diseases are caused by dysfunctional LRO formation and/or motility. Many genes affected by these diseases have been recently identified, revealing new cellular components of the trafficking machinery. Current research reveals how the products of these genes cooperate to generate LROs and how these otherwise diverse organelles are related by the mechanisms through which they form.
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“In the model proposed by Raposo et al. (47,48), the coated endosome (also referred to as a stage 1 melanosome) serves as a critical sorting point between endocytic and pre-melanosomal pathways, from which macromolecules are specifically directed into melanosomal or lysosomal pathways.”
From SLC24A5 encodes a trans-Golgi network protein with potassium-dependent sodium-calcium exchange activity that regulates human epidermal melanogenesis (2008) · cites this paper as [48]
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Cites
NEW CYTOPLASMIC COMPONENTS IN ARTERIAL ENDOTHELIA
Weibel, E. R., & Palade, G. E. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.23.1.101 · Cited by 1,080
Feldmann, J., Callebaut, I., Raposo, G., Dogniaux, S., Bacq, D., Dumont, C., Lambert, N., Ouachée-Chardin, M., Chédeville, G., Tamary, H., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00855-9 · Cited by 935
Self-citationFunctional Amyloid Formation within Mammalian Tissue
Fowler, D. M., Koulov, A. V., Alory, C., Marks, M. S., Balch, W. E., & Kelly, J. W. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040006 · Cited by 847
Self-citationCentrosome polarization delivers secretory granules to the immunological synapse
Stinchcombe, J. C., Majorovits, E., Bossi, G., Fuller, S., & Griffiths, G. M. (2006) · Nature · doi:10.1038/nature05071 · Cited by 599
The melanosome: membrane dynamics in black and white
Marks, M. S., & Seabra, M. C. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096009 · Cited by 464
Self-citationRaposo, G., Tenza, D., Murphy, D. M., Berson, J. F., & Marks, M. S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.809 · Cited by 451
Self-citationLinking Albinism and Immunity: The Secrets of Secretory Lysosomes
Stinchcombe, J. C., Bossi, G., & Griffiths, G. M. (2004) · Science · doi:10.1126/science.1095291 · Cited by 361
Peden, A. A., Oorschot, V. M. J., Hesser, B. A., Austin, C. D., Scheller, R. H., & Klumperman, J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311064 · Cited by 357
Modulation of Receptor Recycling and Degradation by the Endosomal Kinesin KIF16B
Hoepfner, S., Severin, F. F., Cabezas, A., Habermann, B. H., Runge, A., Gillooly, D. J., Stenmark, H., & Zerial, M. (2005) · Cell · doi:10.1016/j.cell.2005.02.017 · Cited by 327
Pmel17 initiates premelanosome morphogenesis within multivesicular bodies
Berson, J. F., Harper, D. C., Tenza, D., Raposo, G., & Marks, M. S. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3451 · Cited by 326
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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
Self-citationvan Niel, G., Charrin, S., Simoes, S., Romao, M., Rochin, L., Saftig, P., Marks, M. S., Rubinstein, E., & Raposo, G. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.08.019 · Cited by 950
Self-citationTrafficking and function of the tetraspanin CD63
Pols, M. S., & Klumperman, J. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.09.020 · Cited by 745
Melanosomes — dark organelles enlighten endosomal membrane transport
Raposo, G., & Marks, M. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2258 · Cited by 623
Self-citationMolecular mechanisms of biogenesis and exocytosis of cytotoxic granules
Basile, G. D. S., Ménasché, G., & Fischer, A. (2010) · Nature reviews. Immunology · doi:10.1038/nri2803 · Cited by 469
Disorders of Lysosome-Related Organelle Biogenesis: Clinical and Molecular Genetics
Huizing, M., Helip‐Wooley, A., Westbroek, W., Gunay‐Aygun, M., & Gahl, W. A. (2008) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.9.081307.164303 · Cited by 429
Frelinger, A. L., Michelson, A. D., & Gremmel, T. (2016) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0035-1564835 · Cited by 368
The biogenesis of lysosomes and lysosome-related organelles
Luzio, J. P., Hackmann, Y., Dieckmann, N. M. G., & Griffiths, G. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016840 · Cited by 330
Wilson Disease Protein ATP7B Utilizes Lysosomal Exocytosis to Maintain Copper Homeostasis
Polishchuk, E. V., Concilli, M., Iacobacci, S., Chesi, G., Pastore, N., Piccolo, P., Paladino, S., Baldantoni, D., van IJzendoorn, S. C. D., Chan, J., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.04.033 · Cited by 284
Lysosome-related organelles: unusual compartments become mainstream
Marks, M. S., Heijnen, H. F. G., & Raposo, G. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.04.008 · Cited by 274
Self-citationFunctional architecture of Weibel-Palade bodies
Valentijn, K. M., Sadler, J. E., Valentijn, J. A., Voorberg, J., & Eikenboom, J. C. J. (2011) · Blood · doi:10.1182/blood-2010-09-267492 · Cited by 277
Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes
Setty, S. R. G., Tenza, D., Sviderskaya, E. V., Bennett, D. C., Raposo, G., & Marks, M. S. (2008) · Nature · doi:10.1038/nature07163 · Cited by 264
Self-citationAcidic calcium stores open for business: expanding the potential for intracellular Ca2+ signaling
Patel, S., & Docampo, R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.02.003 · Cited by 237
Bowman, S. L., Bi‐Karchin, J., Le, L., & Marks, M. S. (2019) · Traffic · doi:10.1111/tra.12646 · Cited by 219
Self-citationSchröder, B. A., Wrocklage, C., Hasilik, A., & Saftig, P. (2010) · PROTEOMICS · doi:10.1002/pmic.201000196 · Cited by 226
Signaling pathways in melanosome biogenesis and pathology
Schiaffino, M. V. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.03.023 · Cited by 213
Notochord vacuoles are lysosome-related organelles that function in axis and spine morphogenesis
Ellis, K., Bagwell, J., & Bagnat, M. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201212095 · Cited by 175
Evolution of intracellular compartmentalization
Diekmann, Y., & Pereira‐Leal, J. B. (2012) · Biochemical Journal · doi:10.1042/bj20120957 · Cited by 175
Thyroid hormone regulates distinct paths to maturation in pigment cell lineages
Saunders, L. M., Mishra, A. K., Aman, A. J., Lewis, V. M., Toomey, M. B., Packer, J. S., Qiu, X., McFaline-Figueroa, J. L., Corbo, J. C., Trapnell, C., et al. (2019) · eLife · doi:10.7554/elife.45181 · Cited by 170
MHC class II molecules on the move for successful antigen presentation
Rocha, N., & Neefjes, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601945 · Cited by 167
Docampo, R., & Moreno, S. N. J. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.05.012 · Cited by 168
Lipid sorting and multivesicular endosome biogenesis
Bissig, C., & Gruenberg, J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016816 · Cited by 151
Ginger, R. S., Askew, S. E., Ogborne, R. M., Wilson, S., Ferdinando, D., Dadd, T., Smith, A. M., Kazi, S., Szerencsei, R. T., Winkfein, R. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707521200 · Cited by 158
Lysosome-related organelles as functional adaptations of the endolysosomal system
Delevoye, C., Marks, M. S., & Raposo, G. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.05.003 · Cited by 174
Self-citationGanesan, A. K., Ho, H., Bodemann, B. O., Petersen, S., Aruri, J., Koshy, S., Richardson, Z., Le, L. Q., Krasieva, T. B., Roth, M. G., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000298 · Cited by 152
Formation and function of Weibel-Palade bodies
Metcalf, D. J., Nightingale, T. D., Zenner, H. L., Lui, W. W. Y., & Cutler, D. F. (2007) · Journal of Cell Science · doi:10.1242/jcs.03494 · Cited by 148
Self-citationMechanisms of Protein Delivery to Melanosomes in Pigment Cells
Sitaram, A., & Marks, M. S. (2012) · Physiology · doi:10.1152/physiol.00043.2011 · Cited by 147
Self-citationGolgi in copper homeostasis: a view from the membrane trafficking field
Polishchuk, R., & Lutsenko, S. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1123-8 · Cited by 134
H ermansky– P udlak syndrome: pigmentary and non‐pigmentary defects and their pathogenesis
Wei, A., & Li, W. (2012) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12051 · Cited by 136
Bultema, J. J., Ambrosio, A. L., Burek, C. L., & Di Pietro, S. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.351908 · Cited by 128
Imaging and imagination: understanding the endo-lysosomal system
van Meel, E., & Klumperman, J. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0384-0 · Cited by 137
Hermansky–Pudlak syndrome: Mutation update
Huizing, M., Malicdan, M. C. V., Wang, J. A., Pri‐Chen, H., Hess, R. A., Fischer, R. E., O’Brien, K., Merideth, M. A., Gahl, W. A., & Gochuico, B. R. (2020) · Human Mutation · doi:10.1002/humu.23968 · Cited by 125
Ray, K., Bobard, A., Danckaert, A., Paz, I., Clair, C., Ehsani, S., Tang, C. M., Sansonetti, P. J., Nhieu, G. T. V., & Enninga, J. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01428.x · Cited by 114
Formation and function of Weibel-Palade bodies
Zhang, Z., & Li, W. (2009) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2009.00882 · Cited by 111
Berruti, G., & Paiardi, C. (2011) · Spermatogenesis · doi:10.4161/spmg.1.2.16820 · Cited by 117
Kloer, D. P., Rojas, R., Ivan, V., Moriyama, K., van Vlijmen, T., Murthy, N., Ghirlando, R., van der Sluijs, P., Hurley, J. H., & Bonifacino, J. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.069088 · Cited by 103
Beer, K. B., & Wehman, A. M. (2016) · Cell Adhesion & Migration · doi:10.1080/19336918.2016.1236899 · Cited by 103
Storage pool diseases illuminate platelet dense granule biogenesis
Ambrosio, A. L., & Pietro, S. M. D. (2016) · Platelets · doi:10.1080/09537104.2016.1243789 · Cited by 94
Interorganelle Communication between Mitochondria and the Endolysosomal System
Soto‐Heredero, G., Baixauli, F., & Mittelbrunn, M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00095 · Cited by 98
Melanosomes on the move: a model to understand organelle dynamics
Hume, A. N., & Seabra, M. C. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391191 · Cited by 99
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Waschbüsch, D., Michels, H., Strassheim, S., Ossendorf, E., Kessler, D., Gloeckner, C. J., & Barnekow, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111632 · Cited by 91
Justo, B. L., & Jasiulionis, M. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179319 · Cited by 89
Salazar, G., Zlatic, S. A., Craige, B., Peden, A. A., Pohl, J., & Faúndez, V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805991200 · Cited by 89
Ryder, P. V., Vistein, R., Gokhale, A., Seaman, M. N., Puthenveedu, M. A., & Faundez, V. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-02-0088 · Cited by 87
Mantegazza, A. R., Guttentag, S. H., Benna, J. E., Sasai, M., Iwasaki, A., Shen, H., Laufer, T. M., & Marks, M. S. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.018 · Cited by 79
Self-citationSubcellular proteomics of Trypanosoma cruzi reservosomes
Sant’Anna, C., Nakayasu, E. S., Pereira, M. G., Lourenço, D. C., de Souza, W., de Almeida, I. C., & Cunha‐e‐Silva, N. L. (2009) · PROTEOMICS · doi:10.1002/pmic.200800730 · Cited by 81
The dynamic properties of intermediate filaments during organelle transport
Chang, L., Barlan, K., Chou, Y.-H., Grin, B., Lakonishok, M., Serpinskaya, A. S., Shumaker, D. K., Herrmann, H. O., Gelfand, V. I., & Goldman, R. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046789 · Cited by 76
Singh, R. K., Mizuno, K., Wasmeier, C., Wavre‐Shapton, S. T., Recchi, C., Catz, S. D., Futter, C. E., Tolmachova, T., Hume, A. N., & Seabra, M. C. (2012) · FEBS Journal · doi:10.1111/febs.12081 · Cited by 83
Gerber, P. P., Cabrini, M., Jancic, C. C., Paoletti, L., Banchio, C., von Bilderling, C., Sigaut, L., Pietrasanta, L. I., Duette, G., Freed, E. O., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201409082 · Cited by 84
Sitaram, A., Piccirillo, R., Palmisano, I., Harper, D. C., Dell’Angelica, E. C., Schiaffino, M. V., & Marks, M. S. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0710 · Cited by 77
Self-citationActin coats and rings promote regulated exocytosis
Nightingale, T. D., Cutler, D. F., & Cramer, L. P. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.03.003 · Cited by 77
Self-citationBLOC-2 targets recycling endosomal tubules to melanosomes for cargo delivery
Dennis, M. K., Mantegazza, A. R., Snir, O. L., Tenza, D., Acosta-Ruiz, A., Delevoye, C., Zorger, R., Sitaram, A., Jesus-Rojas, W. D., Ravichandran, K., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201410026 · Cited by 77
Self-citationGhiani, C. A., & Dell’Angelica, E. C. (2011) · ASN NEURO · doi:10.1042/an20110010 · Cited by 77
Jones, M. L., Murden, S. L., Brooks, C., Maloney, V. K., Manning, R. A., Gilmour, K. C., Bharadwaj, V., de la Fuente, J., Chakravorty, S., & Mumford, A. D. (2013) · BMC Medical Genetics · doi:10.1186/1471-2350-14-42 · Cited by 75
The retromer, sorting nexins and the plant endomembrane protein trafficking
Heucken, N., & Ivanov, R. (2017) · Journal of Cell Science · doi:10.1242/jcs.203695 · Cited by 71
Sitaram, A., Dennis, M. K., Chaudhuri, R., De Jesus-Rojas, W., Tenza, D., Setty, S. R. G., Wood, C. S., Sviderskaya, E. V., Bennett, D. C., Raposo, G., et al. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-06-0509 · Cited by 69
Self-citationBultema, J. J., Boyle, J. A., Malenke, P. B., Martin, F. E., Dell’Angelica, E. C., Cheney, R. E., & Pietro, S. M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.578948 · Cited by 68
Classical autophagy proteins LC3B and ATG4B facilitate melanosome movement on cytoskeletal tracks
Ramkumar, A., Murthy, D., Raja, D. A., Singh, A. K., Krishnan, A., Khanna, S., Vats, A., Thukral, L., Sharma, P., Sivasubbu, S., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1327509 · Cited by 68
Proteomic analysis of extracellular matrix and vesicles
Xiao, Z., Blonder, J., Zhou, M., & Veenstra, T. D. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.11.011 · Cited by 66
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Hammel, I., Lagunoff, D., & Galli, S. J. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01071.x · Cited by 66
Acidocalcisomes: Ultrastructure, Biogenesis, and Distribution in Microbial Eukaryotes
Goodenough, U. W., Heiss, A. A., Roth, R. A., Rusch, J., & Lee, J. (2019) · Protist · doi:10.1016/j.protis.2019.05.001 · Cited by 66
Li, Y., Wang, Y., Zou, L., Tang, X., Yang, Y., Ma, L., Jia, Q., Ni, Q., Liu, S.-Q., Tang, L., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.027 · Cited by 65
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Zhu, G.-D., Salazar, G., Zlatic, S. A., Fiza, B., Doucette, M. M., Heilman, C. J., Levey, A. I., Faúndez, V., & L’Hernault, S. W. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0728 · Cited by 63
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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
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Fraile‐Ramos, A., Cepeda, V., Elstak, E., & van der Sluijs, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015318 · Cited by 63
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Braun, V., Deschamps, C., Raposo, G., Benaroch, P., Benmerah, A., Chavrier, P., & Niedergang, F. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0392 · Cited by 65
Self-citationAll Trypanosoma cruzi developmental forms present lysosome-related organelles
Sant’Anna, C., Parussini, F., Lourenço, D. C., de Souza, W., Cazzulo, J. J., & Cunha‐e‐Silva, N. L. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0486-8 · Cited by 60
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Jani, R. A., Purushothaman, L. K., Rani, S., Bergam, P., & Setty, S. R. G. (2015) · Journal of Cell Science · doi:10.1242/jcs.171165 · Cited by 60
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Bello‐Morales, R., Crespillo, A. J., Fraile‐Ramos, A., Tabarés, E., Alcina, A., & López‐Guerrero, J. A. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-265 · Cited by 60
Naß, J., Terglane, J., & Gerke, V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.813995 · Cited by 60
Form and Function of Exosome-Associated Long Non-coding RNAs in Cancer
Hewson, C., & Morris, K. V. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_486 · Cited by 59
An early endosome–derived retrograde trafficking pathway promotes secretory granule maturation
Ma, C.-I. J., Yang, Y., Kim, T., Chen, C., Polevoy, G., Vissa, M., Burgess, J., & Brill, J. A. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201808017 · Cited by 59
Meng, R., Wang, Y., Yao, Y., Zhang, Z., Harper, D. C., Heijnen, H. F. G., Sitaram, A., Li, W., Raposo, G., Weiss, M. J., et al. (2012) · Blood · doi:10.1182/blood-2011-11-389551 · Cited by 58
Self-citationFan, J., Dong, H., Hu, M., Wang, J., Zhang, H., Zhu, H., Sun, W. C., & Peng, X. (2013) · Chemical Communications · doi:10.1039/c3cc48043g · Cited by 57
Role of AP1 and Gadkin in the traffic of secretory endo-lysosomes
Laulagnier, K., Schieber, N. L., Maritzen, T., Haucke, V., Parton, R. G., & Gruenberg, J. E. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-03-0193 · Cited by 57
Dysbindin-1 and Its Protein Family
Talbot, K., Ong, W., Blake, D. J., Tang, J., Louneva, N., Carlson, G. C., & Arnold, S. E. (2009) · Springer eBooks · doi:10.1007/978-0-387-30410-6_5 · Cited by 57
Bultema, J. J., & Pietro, S. M. D. (2013) · Small GTPases · doi:10.4161/sgtp.22349 · Cited by 58
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Huizing, M., Pederson, B., Hess, R. A., Griffin, A., Helip‐Wooley, A., Westbroek, W., Dorward, H. M., O’Brien, K., Golas, G. A., Tsilou, E., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2008.065961 · Cited by 54
Gremmel, T., Frelinger, A. L., & Michelson, A. D. (2024) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0044-1786387 · Cited by 56
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Ren, M., Xu, Y., Erdjument‐Bromage, H., Donelian, A., Phoon, C. K. L., Terada, N., Strathdee, D., Neubert, T. A., & Schlame, M. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201808131 · Cited by 51
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Damek-Poprawa, M., Diemer, T., Lopes, V. S., Lillo, C., Harper, D. C., Marks, M. S., Wu, Y., Sparrow, J. R., Rachel, R. A., Williams, D. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808857200 · Cited by 50
Self-citationIshida, M., Ohbayashi, N., & Fukuda, M. (2015) · Scientific Reports · doi:10.1038/srep08238 · Cited by 49
Truschel, S. T., Simoes, S., Setty, S. R. G., Harper, D. C., Tenza, D., Thomas, P. C., Herman, K. E., Sackett, S. D., Cowan, D. C., Theos, A. C., et al. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00955.x · Cited by 48
Self-citationMurrell‐Lagnado, R. D., & Frick, M. (2019) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2019.03.002 · Cited by 45
Campbell, E. M., & Fares, H. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-40 · Cited by 44
Rab9A is required for delivery of cargo from recycling endosomes to melanosomes
Mahanty, S., Ravichandran, K., Chitirala, P., Prabha, J., Jani, R. A., & Setty, S. R. G. (2015) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12434 · Cited by 45
Stimulated release of intraluminal vesicles from Weibel-Palade bodies
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Self-citation
Metadata
- Authors
- Raposo, G., Marks, M. S., & Cutler, D. F.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Pennsylvania (US)
- MRC Laboratory for Molecular Cell Biology (GB)
- Corresponding author
- Raposo, Graça
- Cutler, Daniel F
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 19
- Issue
- 4
- Pages
- 394-401
- ISSN
- 0955-0674 (ISSN-L)
- PMC
- PMC2782641
- OpenAlex
- W2062800617
- Cited by
- 215
- References
- 59
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 10 · 2023: 4 · 2022: 8 · 2021: 14 · 2020: 5 · 2019: 9 · 2018: 4 · 2017: 10 · 2016: 17 · 2015: 11 · 2014: 10 · 2013: 20 · 2012: 16
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Centre National de la Recherche Scientifique
- National Institutes of Health (5r01ar048155-13)
- Medical Research Council
- National Eye Institute (R01EY015625)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01 AR-048155)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- lysosome-related organelles, late endosomes, lysosomes, post-Golgi trafficking, organelle biogenesis, organelle motility, lysosomal storage disease
- MeSH terms
- rab27 GTP-Binding Proteins, Animals, Cell Compartmentation, Golgi Apparatus, Humans, Lysosomes, Endosomes, Organelles, Melanosomes, rab GTP-Binding Proteins, Protein Sorting Signals
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