Functional involvement of Rab1A in microtubule-dependent anterograde melanosome transport in melanocytes
Open accessAbstract
Melanosomes are transported to the cell periphery of melanocytes by coordination between bidirectional microtubule-dependent movements and unidirectional actin-dependent movement. Although both the mechanism of the actin-dependent melanosome transport and the mechanism of the microtubule-dependent retrograde melanosome transport in mammalian skin melanocytes have already been determined, almost nothing is known about the mechanism of the microtubule-dependent anterograde melanosome transport. Small GTPase Rab proteins are common regulators of membrane traffic in all eukaryotes, and in this study we performed genome-wide screening for Rab proteins that are involved in anterograde melanosome transport by expressing 60 different constitutive active (and negative) mutants and succeeded in identifying Rab1A, originally described as a Golgi-resident Rab, as a prime candidate. Endogenous Rab1A protein was found to be localized on mature melanosomes in melanocytes, and its functional ablation either by siRNA-mediated knockdown or by overexpression of a cytosolic form of Rab1A-GTPase-activating protein/TBC1D20 induced perinuclear melanosome aggregation. The results of time-lapse imaging further revealed that long-range anterograde melanosome movements were specifically suppressed in Rab1A-deficient melanocytes, whereas retrograde melanosome transport occurred normally. Taken together, these findings indicate that Rab1A is the first crucial component of the anterograde melanosome transport machinery to be identified in mammalian skin melanocytes.
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Rab1 interacts with SKIP and kinesin 1 to regulate melanosome anterograde transport.
“The Ras-related protein in brain (Rab) 1, which mediates endoplasmic reticulum (ER)-Golgi trafficking, interacts with the SifA and kinesin-interacting protein (SKIP), as well as the anterograde microtubule-dependent motor kinesin 1, to regulate melanosome anterograde transport [ 35 , 36 ]”
From Melanin's Journey from Melanocytes to Keratinocytes: Uncovering the Molecular Mechanisms of Melanin Transfer and Processing (2023) · cites this paper as [35]
The Introduction reports that Rab1A regulates ER-to-Golgi trafficking, and the Discussion reports Rab1A binding to SKIP and SKIP binding to kinesin-1. The paper also finds that Rab1A is involved in anterograde melanosome transport, but the Discussion calls transport by a Rab1A–SKIP–kinesin-1 complex a possibility requiring further work, not an established mechanism. No page numbers were available in our copy. (LLM, conf=0.90)
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Cites
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413 · see citing works
Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.
Stenmark, H., Parton, R. G., Steele‐Mortimer, O., Lütcke, A., Gruenberg, J., & Zerial, M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06381.x · Cited by 968 · see citing works
Melanosomes — dark organelles enlighten endosomal membrane transport
Raposo, G., & Marks, M. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2258 · Cited by 587 · see citing works
Interaction of a Golgi-Associated Kinesin-Like Protein with Rab6
Échard, A., Jollivet, F., Martinez, O., Lacapère, J.-J., Rousselet, A., Janoueix‐Lerosey, I., & Goud, B. (1998) · Science · doi:10.1126/science.279.5350.580 · Cited by 518 · see citing works
Bennett, D. C., Cooper, P. J., & Hart, I. R. (1987) · International Journal of Cancer · doi:10.1002/ijc.2910390324 · Cited by 484 · see citing works
Rab1 Recruitment of p115 into a cis-SNARE Complex: Programming Budding COPII Vesicles for Fusion
Allan, B. B., Moyer, B. D., & Balch, W. E. (2000) · Science · doi:10.1126/science.289.5478.444 · Cited by 458 · see citing works
Identification of an organelle receptor for myosin-Va
Wu, X., Rao, K., Zhang, H., Wang, F., Sellers, J. R., Matesic, L. E., Copeland, N. G., Jenkins, N. A., & Hammer, J. A. (2002) · Nature Cell Biology · doi:10.1038/ncb760 · Cited by 455 · see citing works
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 452 · see citing works
Wu, X., Bowers, B., Rao, K., Wei, Q., & Hammer, J. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1899 · Cited by 419 · see citing works
A mutation in Rab27a causes the vesicle transport defects observed in ashen mice
Wilson, S. M., Yip, R., Swing, D. A., O’Sullivan, T. N., Zhang, Y., Novak, E. K., Swank, R. T., Russell, L. B., Copeland, N. G., & Jenkins, N. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140212797 · Cited by 406 · see citing works
Slac2-a/Melanophilin, the Missing Link between Rab27 and Myosin Va
Fukuda, M., Kuroda, T. S., & Mikoshiba, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200005200 · Cited by 364 · see citing works
Self-citationArl8 and SKIP Act Together to Link Lysosomes to Kinesin-1
Rosa-Ferreira, C., & Munro, S. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.007 · Cited by 361 · see citing works
Membrane traffic in the secretory pathway
Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 359 · see citing works
Self-citationA Family of Rab27-binding Proteins
Strom, M., Hume, A. N., Tarafder, A. K., Barkagianni, E., & Seabra, M. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202574200 · Cited by 324 · see citing works
Dynactin is required for bidirectional organelle transport
Deacon, S. W., Serpinskaya, A. S., Vaughan, P. S., Fanárraga, M. L., Vernos, I., Vaughan, K. T., & Gelfand, V. I. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200210066 · Cited by 311 · see citing works
The Intracellular Fate of Salmonella Depends on the Recruitment of Kinesin
Boucrot, E., Henry, T., Borg, J., Gorvel, J., & Méresse, S. (2005) · Science · doi:10.1126/science.1110225 · Cited by 237 · see citing works
Niwa, S., Tanaka, Y., & Hirokawa, N. (2008) · Nature Cell Biology · doi:10.1038/ncb1785 · Cited by 232 · see citing works
Linking molecular motors to membrane cargo
Akhmanova, A. S., & Hammer, J. A. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.008 · Cited by 218 · see citing works
Versatile Role of Rab27 in Membrane Trafficking: Focus on the Rab27 Effector Families
Fukuda, M. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi002 · Cited by 215 · see citing works
Self-citationKuroda, T. S., Fukuda, M., Ariga, H., & Mikoshiba, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112414200 · Cited by 211 · see citing works
Self-citationTBC proteins: GAPs for mammalian small GTPase Rab?
Fukuda, M. (2011) · Bioscience Reports · doi:10.1042/bsr20100112 · Cited by 207 · see citing works
Self-citationAnterograde Transport of TrkB in Axons Is Mediated by Direct Interaction with Slp1 and Rab27
Arimura, N., Kimura, T., Nakamuta, S., Taya, S., Funahashi, Y., Hattori, A., Shimada, A., Ménager, C., Kawabata, S., Fujii, K., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.03.005 · Cited by 202 · see citing works
Self-citationHaas, A. K., Yoshimura, S.-I., Stephens, D. J., Preisinger, C., Fuchs, E., & Barr, F. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.014225 · Cited by 201 · see citing works
Proteomic and Bioinformatic Characterization of the Biogenesis and Function of Melanosomes
Chi, A., Valencia, J. C., Hu, Z.-Z., Watabe, H., Yamaguchi, H., Mangini, N. J., Huang, H., Canfield, V. A., Cheng, K. C., Yang, F., et al. (2006) · Journal of Proteome Research · doi:10.1021/pr060363j · Cited by 199 · see citing works
Tsuboi, T., & Fukuda, M. (2006) · Journal of Cell Science · doi:10.1242/jcs.02962 · Cited by 188 · see citing works
Self-citationGriscelli syndrome: a model system to study vesicular trafficking
Gele, M. V., Dynoodt, P., & Lambert, J. (2009) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2009.00558.x · Cited by 184 · see citing works
Tuma, M. C., Zill, A. T., Bot, N. L., Vernos, I., & Gelfand, V. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1547 · Cited by 178 · see citing works
Schlager, M. A., Kapitein, L. C., Grigoriev, I., Burzynski, G. M., Wulf, P. S., Keijzer, N., de Graaff, E., Fukuda, M., Shepherd, I. T., Akhmanova, A., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.51 · Cited by 165 · see citing works
Self-citationMutation of melanosome protein RAB38 in chocolate mice
Loftus, S. K., Larson, D. M., Baxter, L. L., Antonellis, A., Chen, Y., Wu, X., Jiang, Y. Y., Bittner, M. L., Hammer, J. A., & Pavan, W. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072087599 · Cited by 163 · see citing works
Itoh, T., Satoh, M., Kanno, E., & Fukuda, M. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.00997.x · Cited by 158 · see citing works
Self-citationKuroda, T. S., & Fukuda, M. (2004) · Nature Cell Biology · doi:10.1038/ncb1197 · Cited by 158 · see citing works
Self-citationFunctional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome
Barral, D. C., Ramalho, J. S., Anders, R., Hume, A. N., Knapton, H. J., Tolmachova, T., Collinson, L., Goulding, D., Authi, K. S., & Seabra, M. C. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15058 · Cited by 157 · see citing works
Functional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome
Barral, D. C., Ramalho, J. S., Anders, R., Hume, A. N., Knapton, H. J., Tolmachova, T., Collinson, L., Goulding, D., Authi, K. S., & Seabra, M. C. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215058 · Cited by 155 · see citing works
The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking
Kauppi, M., Simonsen, A., Bremnes, B., Vieira, A. V., Callaghan, J. M., Stenmark, H., & Olkkonen, V. M. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.5.899 · Cited by 151 · see citing works
Melanophilin, the Product of the Leaden Locus, is Required for Targeting of Myosin‐Va to Melanosomes
Provance, D. W., James, T. L., & Mercer, J. A. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.030205.x · Cited by 133 · see citing works
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 · see citing works
Kuroda, T. S., Ariga, H., & Fukuda, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5245-5255.2003 · Cited by 122 · see citing works
Self-citationGolgin‐84 is a rab1 Binding Partner Involved in Golgi Structure
Satoh, A., Wang, Y., Malsam, J., Beard, M., & Warren, G. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00103.x · Cited by 121 · see citing works
Chapter 6 New Insights into Melanosome Transport in Vertebrate Pigment Cells
Aspengren, S., Hedberg, D., Sköld, H. N., & Wallin, M. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01606-7 · Cited by 120 · see citing works
Ueno, H., Huang, X., Tanaka, Y., & Hirokawa, N. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.11.008 · Cited by 116 · see citing works
Multiple regions contribute to membrane targeting of Rab GTPases
Ali, B. R., Wasmeier, C., Lamoreux, L., Strom, M., & Seabra, M. C. (2004) · Journal of Cell Science · doi:10.1242/jcs.01542 · Cited by 116 · see citing works
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 · see citing works
Rab GTPases and microtubule motors
Horgan, C. P., & McCaffrey, M. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391202 · Cited by 111 · see citing works
Dumont, A., Boucrot, E., Drevensek, S., Daire, V., Gorvel, J., Poüs, C., Holden, D. W., & Méresse, S. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01069.x · Cited by 107 · see citing works
Varp Is a Novel Rab32/38-binding Protein That Regulates Tyrp1 Trafficking in Melanocytes
Tamura, K., Ohbayashi, N., Maruta, Y., Kanno, E., Itoh, T., & Fukuda, M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1161 · Cited by 105 · see citing works
Self-citationRegulation of Integrin β1 Recycling to Lipid Rafts by Rab1a to Promote Cell Migration
Wang, C., Yoo, Y., Fan, H., Kim, E., Guan, K., & Guan, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.141440 · Cited by 100 · see citing works
Beaumont, K. A., Hamilton, N. A., Moores, M. T., Brown, D. L., Ohbayashi, N., Cairncross, O., Cook, A. L., Smith, A. G., Misaki, R., Fukuda, M., et al. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01172.x · Cited by 97 · see citing works
Self-citationMatsui, T., Ohbayashi, N., & Fukuda, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.370544 · Cited by 90 · see citing works
Self-citationIdentification of EPI64 as a GTPase-activating Protein Specific for Rab27A
Itoh, T., & Fukuda, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603808200 · Cited by 84 · see citing works
Self-citationThe Salmonella virulence protein SifA is a G protein antagonist
Jackson, L. K., Nawabi, P., Hentea, C., Roark, E. A., & Haldar, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801872105 · Cited by 81 · see citing works
Role of Rab family GTPases and their effectors in melanosomal logistics
Ohbayashi, N., & Fukuda, M. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs009 · Cited by 73 · see citing works
Self-citationTamura, K., Ohbayashi, N., Ishibashi, K., & Fukuda, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.191205 · Cited by 70 · see citing works
Self-citationFukuda, M., Kobayashi, H., Ishibashi, K., & Ohbayashi, N. (2011) · Cell Structure and Function · doi:10.1247/csf.11001 · Cited by 68 · see citing works
Self-citationProteomic analysis of endocytic vesicles: Rab1a regulates motility of early endocytic vesicles
Mukhopadhyay, A., Nieves, E., Che, F., Wang, J. C. Y., Jin, L., Murray, J. W., Gordon, K. M., Angeletti, R. H., & Wolkoff, A. W. (2011) · Journal of Cell Science · doi:10.1242/jcs.079020 · Cited by 66 · see citing works
Rab8 Regulates the Actin-based Movement of Melanosomes
Chabrillat, M. L., Wilhelm, C., Wasmeier, C., Sviderskaya, E. V., Louvard, D., & Coudrier, E. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-09-0770 · Cited by 65 · see citing works
Bahadoran, P., Buscà, R., Chiavérini, C., Westbroek, W., Lambert, J., Bille, K., Valony, G., Fukuda, M., Naeyaert, J. M., Ortonne, J. P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211996200 · Cited by 63 · see citing works
Self-citationOhbayashi, N., Maruta, Y., Ishida, M., & Fukuda, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.094185 · Cited by 61 · see citing works
Self-citationDilute suppressor, a new suppressor gene in the house mouse
Sweet, H. O. (1983) · Journal of Heredity · doi:10.1093/oxfordjournals.jhered.a109794 · Cited by 57 · see citing works
Decreased basal mucus secretion by Slp2‐a‐deficient gastric surface mucous cells
Saegusa, C., Tanaka, T., Tani, S., Itohara, S., Mikoshiba, K., & Fukuda, M. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.00964.x · Cited by 50 · see citing works
Self-citationdsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice
O’Sullivan, T. N., Wu, X., Rachel, R. A., Huang, J.-D., Swing, D. A., Matesic, L. E., Hammer, J. A., Copeland, N. G., & Jenkins, N. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407339101 · Cited by 46 · see citing works
Mori, Y., Matsui, T., Furutani, Y., Yoshihara, Y., & Fukuda, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.314385 · Cited by 45 · see citing works
Self-citationFukuda, M. (2010) · PubMed · doi:10.14670/hh-25.1473 · Cited by 27 · see citing works
Self-citationA mouse TRAPP-related protein is involved in pigmentation
Gwynn, B., Smith, R. S., Rowe, L. B., Taylor, B. A., & Peters, L. L. (2006) · Genomics · doi:10.1016/j.ygeno.2006.04.002 · Cited by 26 · see citing works
The LRRK2-related Roco kinase Roco2 is regulated by Rab1A and controls the actin cytoskeleton
Kicka, S., Shen, Z., Annesley, S. J., Fisher, P. R., Lee, S. D., Briggs, S. P., & Firtel, R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0937 · Cited by 20 · see citing works
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Mutations in the deubiquitinase gene USP8 cause Cushing's disease
Reincke, M., Sbiera, S., Hayakawa, A., Theodoropoulou, M., Oßwald, A., Beuschlein, F., Meitinger, T., Mizuno-Yamasaki, E., Kawaguchi, K., Saeki, Y., et al. (2014) · Nature Genetics · doi:10.1038/ng.3166 · Cited by 599 · see citing works
Soo, 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 117 · see citing works
Bento-Lopes, L., Cabaço, L. C., Charneca, J., Neto, M. V., Seabra, M. C., & Barral, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411289 · Cited by 114 · see citing works
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Fukuda, M. (2020) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12931 · Cited by 76 · see citing works
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Tian, X., Cui, Z., Liu, S., Zhou, J., & Cui, R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107707 · Cited by 75 · see citing works
Zhang, Q., Pan, Y., Zeng, B., Zheng, X., Wang, H., Shen, X., Li, H., Jiang, Q., Zhao, J., Meng, Z.-X., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0190-3 · Cited by 73 · see citing works
Ypt1/Rab1 regulates Hrr25/CK1δ kinase activity in ER–Golgi traffic and macroautophagy
Wang, J., Davis, S., Menon, S., Zhang, J., Ding, J., Cervantes, S., Miller, E. A., Jiang, Y., & Ferro‐Novick, S. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201408075 · Cited by 72 · see citing works
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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 67 · see citing works
Aizawa, M., & Fukuda, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.669242 · Cited by 66 · see citing works
Self-citationLangemeyer, L., Bastos, R. N., Cai, Y., Itzen, A., Reinisch, K. M., & Barr, F. A. (2014) · eLife · doi:10.7554/elife.01623 · Cited by 66 · see citing works
Yang, Y., Hou, N., Wang, X., Wang, L., Chang, S., He, K., Zhao, Z., Zhao, X., Song, T., & Huang, C. Y. (2015) · Oncotarget · doi:10.18632/oncotarget.3970 · Cited by 64 · see citing works
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Self-citationMankouri, J., Walter, C. T., Stewart, H., Bentham, M., Park, W. S., Heo, W. D., Fukuda, M., Griffin, S. D. C., & Harris, M. (2016) · Journal of Virology · doi:10.1128/jvi.00826-16 · Cited by 52 · see citing works
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 · see citing works
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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 45 · see citing works
Self-citationVillarroel‐Campos, D., Henríquez, D. R., Bodaleo, F. J., Oguchi, M. E., Bronfman, F. C., Fukuda, M., & González-Billault, C. E. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4064-15.2016 · Cited by 42 · see citing works
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Quan, Y. H., Song, Q., Wang, J., Zhao, L., Lv, J., & Gong, S. (2017) · Tumor Biology · doi:10.1177/1010428317697565 · Cited by 31 · see citing works
Mizushima, T., Jiang, G., Kawahara, T., Li, P., Han, B., Inoue, S., Ide, H., Kato, I., Jalalizadeh, M., Miyagi, E., et al. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0050 · Cited by 31 · see citing works
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Yatsu, A., Shimada, H., Ohbayashi, N., & Fukuda, M. (2015) · Biology Open · doi:10.1242/bio.201411114 · Cited by 28 · see citing works
Self-citationZhang, J., Shen, Y., Xu, X., Dai, Y., & Li, J. (2020) · Marine Biotechnology · doi:10.1007/s10126-020-09994-z · Cited by 28 · see citing works
Ishida, M., Saki, A., Ohbayashi, N., & Fukuda, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.552281 · Cited by 26 · see citing works
Self-citationUemura, T., Kametaka, S., & Waguri, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-19542-4 · Cited by 28 · see citing works
Rab7B/42 is functionally involved in protein degradation on melanosomes in keratinocytes
Marubashi, S., & Fukuda, M. (2020) · Cell Structure and Function · doi:10.1247/csf.19039 · Cited by 25 · see citing works
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Toll‐like receptors 2 and 3 enhance melanogenesis and melanosome transport in human melanocytes
Koike, S., Yamasaki, K., Yamauchi, T., Inoue, M., Shimada‐Omori, R., Tsuchiyama, K., & Aiba, S. (2018) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12703 · Cited by 25 · see citing works
Dual function of Rab1A in secretion and autophagy: hypervariable domain dependence
Gyurkovska, V., Murtazina, R., Zhao, S. F., Shikano, S., Okamoto, Y., & Segev, N. (2023) · Life Science Alliance · doi:10.26508/lsa.202201810 · Cited by 25 · see citing works
Oguchi, M. E., Okuyama, K., Homma, Y., & Fukuda, M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012233 · Cited by 24 · see citing works
Self-citationARHGEF10 directs the localization of Rab8 to Rab6-positive executive vesicles
Shibata, S., Kawanai, T., Hara, T., Yamamoto, A., Chaya, T., Tokuhara, Y., Tsuji, C., Sakai, M., Tachibana, T., & Inagaki, S. (2016) · Journal of Cell Science · doi:10.1242/jcs.186817 · Cited by 22 · see citing works
Hatoyama, Y., Homma, Y., Hiragi, S., & Fukuda, M. (2021) · Journal of Cell Science · doi:10.1242/jcs.259184 · Cited by 21 · see citing works
Self-citationKumar, R., Francis, V., Kulasekaran, G., Khan, M. Z., Armstrong, G. A. B., & McPherson, P. S. (2022) · Science Advances · doi:10.1126/sciadv.abk3088 · Cited by 19 · see citing works
Inhibition of endocytic vesicle fusion by Plk1-mediated phosphorylation of vimentin during mitosis
Ikawa, K., Satou, A., Fukuhara, M., Matsumura, S., Sugiyama, N., Goto, H., Fukuda, M., Inagaki, M., Ishihama, Y., & Toyoshima, F. (2013) · Cell Cycle · doi:10.4161/cc.26866 · Cited by 20 · see citing works
Self-citationInefficient recruitment of kinesin-1 to melanosomes precludes it from facilitating their transport
Robinson, C. L., Evans, R. D., Briggs, D. A., Ramalho, J. S., & Hume, A. N. (2017) · Journal of Cell Science · doi:10.1242/jcs.186064 · Cited by 17 · see citing works
Microtubule Motor Transport of Organelles in a Specialized Epithelium: The RPE
Hazim, R. A., & Williams, D. S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.852468 · Cited by 10 · see citing works
Rab20, a novel Rab small GTPase that negatively regulates neurite outgrowth of PC12 cells
Oguchi, M. E., Etoh, K., & Fukuda, M. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.10.056 · Cited by 11 · see citing works
Self-citationM-INK, a novel tool for visualizing melanosomes and melanocores
Ishida, M., Marubashi, S., & Fukuda, M. (2016) · The Journal of Biochemistry · doi:10.1093/jb/mvw100 · Cited by 8 · see citing works
Self-citationFukuda, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.20020-5 · Cited by 5 · see citing works
Self-citationLi, Y., Xia, H., Chen, L., & Zhang, X. (2017) · PubMed Central · Cited by 4 · see citing works
kinesin recruitment by adapter SKIP on melanosomes is dynamically controlled by LC3B phosphorylationPreprint
Subramaniam, Y. J., Murthy, D., Raja, D. A., Ramkumar, A., Sivasubbu, S., McEwan, D. G., Gokhale, R. S., & Natarajan, V. T. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.11.434917 · Cited by 4 · see citing works
Insights into lysosome-related organelle biogenesis: melanosome as a model organelle
Barral, D. C., Delevoye, C., Larue, L., Seabra, M. C., Raposo, G., & Setty, S. R. G. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1758081 · Cited by 3 · see citing works
Molecular mechanism of melanin transfer from donor melanocytes to recipient keratinocytes
Festas, T. C. (2015) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Wedegaertner, P., & Randolph, C. E. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736177314.793564858
Williams, J. A. (2016) · doi:10.3998/panc.2016.4
Williams, J. A. (2011) · doi:10.3998/panc.2010.8
Kumar, R., Francis, V., Khan, M. Z., Aguila, A., Kulasekaran, G., & McPherson, P. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.21.554162
Khan, M. Z., Kumar, R., Trempe, J.-F., Francis, V., Banks, E., Ayoubi, R., Luna, L. A., & McPherson, P. S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110588
Study of the role of Rab proteins and their effectors on Tunneling nanotubes
Bhat, S. (2019) · theses.fr (ABES) · doi:10.70675/7fee92a1zc615z4de9z87cdz4ac590863df0
- Authors
- Ishida, M., Ohbayashi, N., Maruta, Y., Ebata, Y., & Fukuda, M.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Fukuda, Mitsunori
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2012-01-01
- Volume
- 125
- Issue
- Pt 21
- Pages
- 5177-87
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2061500309
- Cited by
- 49
- References
- 64
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 7 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 8 · 2014: 4 · 2013: 2
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (24570206)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- Rab1A, melanosome transport, anterograde transport, melanocytes, microtubule transport, retrograde transport, Rab GTPases, membrane trafficking, melanosome aggregation, Golgi apparatus
- MeSH terms
- Animals, Cell Line, Humans, Melanocytes, Microscopy, Fluorescence, Microtubules, Mutagenesis, Site-Directed, Protein Isoforms, Mutation, Missense, Melanosomes, rab1 GTP-Binding Proteins, Protein Transport, RNA, Small Interfering, Green Fluorescent Proteins, Mice, Gene Knockdown Techniques
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