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Rab27a and MyoVa are the primary Mlph interactors regulating melanosome transport in melanocytes
Open accessAbstract
Melanosome transport in melanocytes is a model system for the study of cytoskeletal regulation of intracellular transport. Melanophilin (Mlph) is a Rab27a- and myosin Va (MyoVa)-binding protein that regulates this process. Using yeast two-hybrid screening, we identified MT plus-end binding protein (EB1) as a melanocyte-expressed Mlph-interacting protein. To address the role of EB1 versus Rab27a and MyoVa interactions in Mlph targeting and function, we used siRNA and Mlph mutations to specifically disrupt each interaction in cultured melanocytes. Using the Mlph R35W mutant that blocks Mlph-Rab27a interaction and Rab27a siRNA we show this interaction is required for melanosome targeting and stability of Mlph. Mutants and siRNA that affect Mlph-MyoVa and Mlph-EB1 interactions reveal that while neither MyoVa nor EB1 affect Mlph targeting to melanosomes, MyoVa but not EB1 interaction is required for transport of melanosomes to peripheral dendrites. We propose that Mlph is targeted to and/or stabilised on melanosomes by Rab27a, and then recruits MyoVa, which provides additional stability to the complex and allows melanosomes to transfer from MT to actin-based transport and achieve peripheral distribution. EB1 appears to be non-essential to this process in cultured melanocytes, which suggests that it plays a redundant role and/or is required for melanocyte/keratinocyte contacts and melanosome transfer.
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At the cell periphery, melanosomes are anchored to cortical actin and transported to the plasma membrane by a tripartite complex of Rab27a, melanophilin, and myosin Va.
“At the cell periphery, melanosomes are anchored to the cortical actin network and unidirectionally transported to the plasma membrane by the tripartite complex composed of the secretory protein Rab27a, the adaptor protein melanophilin, and the actin-dependent motor protein myosin Va [ 40 , 41 ]”
From Melanin's Journey from Melanocytes to Keratinocytes: Uncovering the Molecular Mechanisms of Melanin Transfer and Processing (2023) · cites this paper as [41]
The Introduction (page unavailable) describes melanosomes being retained in peripheral dendrites through an actin-associated mechanism and making short myosin-driven movements toward the plasma membrane. The section on complex stability identifies Rab27a, melanophilin and myosin Va as a tripartite melanosome-associated complex. The paper does not establish the citing sentence’s stronger claim that transport is unidirectional. (LLM, conf=0.86)
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Cites
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430
Schiestl, R. H., & Gietz, R. D. (1989) · Current Genetics · doi:10.1007/bf00340712 · Cited by 2,143
Methods in Yeast Genetics: A Laboratory Course Manual
Rose, M. D., Winston, F., & Hieter, P. (1990) · Medical Entomology and Zoology · Cited by 1,894
The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.Preprint
Durfee, T. J., Becherer, K., Chen, P., Yeh, S. H., Yang, Y., Kilburn, A. E., Lee, W., & Elledge, S. J. (1993) · Genes & Development · doi:10.1101/gad.7.4.555 · Cited by 1,451
Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
Fromont‐Racine, M., Rain, J., & Legrain, P. (1997) · Nature Genetics · doi:10.1038/ng0797-277 · Cited by 930
Shaw, R. M., Fay, A. J., Puthenveedu, M. A., von Zastrow, M., Jan, Y. N., & Jan, L. Y. (2007) · Cell · doi:10.1016/j.cell.2006.12.037 · Cited by 487
The Color Loci of Mice – A Genetic Century
Bennett, D. C., & Lamoreux, M. L. (2003) · Pigment Cell Research · doi:10.1034/j.1600-0749.2003.00067.x · Cited by 486
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
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
Self-citationWu, 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
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
Ménasché, G., Ho, C. H., Sanal, Ö., Feldmann, J., Tezcan, İ., Ersoy, F., Houdusse, A., Fischer, A., & Basile, G. D. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18264 · Cited by 355
Rab27a Regulates the Peripheral Distribution of Melanosomes in Melanocytes
Hume, A. N., Collinson, L., Rapak, A., Gomes, A. Q., Hopkins, C. R., & Seabra, M. C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.795 · Cited by 333
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
Self-citationMénasché, G., Ho, C. H., Sanal, Ö., Feldmann, J., Tezcan, İ., Ersoy, F., Houdusse, A., Fischer, A., & Basile, G. D. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318264 · Cited by 287
The Quest for the Mechanism of Melanin Transfer
Bossche, K. V. D., Naeyaert, J., & Lambert, J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00425.x · Cited by 246
Morrison, E. E., Wardleworth, B. N., Askham, J. M., Markham, A. F., & Meredith, D. M. (1998) · Oncogene · doi:10.1038/sj.onc.1202247 · Cited by 218
Slep, K. C., Rogers, S. L., Elliott, S. L., Ohkura, H., Kolodziej, P. A., & Vale, R. D. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410114 · Cited by 207
Crystal Structure of the Amino-terminal Microtubule-binding Domain of End-binding Protein 1 (EB1)
Hayashi, I., & Ikura, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305773200 · Cited by 202
Askham, J. M., Vaughan, K. T., Goodson, H. V., & Morrison, E. E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-01-0061 · Cited by 190
Berrueta, L., Kraeft, S., Tirnauer, J. S., Schuyler, S. C., Chen, L. B., HILL, D. E., Pellman, D. S., & Bierer, B. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10596 · Cited by 179
Melanophilin directly links Rab27a and myosin Va through its distinct coiled‐coil regions
Nagashima, K., Torii, S., Yi, Z., Igarashi, M., Okamoto, K., Takeuchi, T., & Izumi, T. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02634-0 · Cited by 159
Kuroda, T. S., & Fukuda, M. (2004) · Nature Cell Biology · doi:10.1038/ncb1197 · Cited by 158
The leaden Gene Product Is Required with Rab27a to Recruit Myosin Va to Melanosomes in Melanocytes
Hume, A. N., Collinson, L., Hopkins, C. R., Strom, M., Barral, D. C., Bossi, G., Griffiths, G. M., & Seabra, M. C. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.030305.x · Cited by 154
Self-citationStructural insights into the EB1–APC interaction
Srinivas, H., John, C., Kostrewa, D., Winkler, F. K., & Steinmetz, M. O. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600529 · Cited by 151
TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends
Vaughan, K. T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200509150 · Cited by 142
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
Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150Glued Complex
Hayashi, I., Wilde, A., Mal, T. K., & Ikura, M. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.034 · Cited by 130
Kinesin participates in melanosomal movement along melanocyte dendrites
Hara, M., Yaar, M., Byers, H. R., Goukassian, D., Gonsalves, J., Gilchrest, B. A., & Fine, R. E. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00894.x · Cited by 127
Kuroda, T. S., Ariga, H., & Fukuda, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5245-5255.2003 · Cited by 122
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
Self-citationMelanophilin and myosin Va track the microtubule plus end on EB1
Wu, X., Tsan, G. L., & Hammer, J. A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503028 · Cited by 100
Rab7 and Rab27a control two motor protein activities involved in melanosomal transport
Jordens, I., Westbroek, W., Marsman, M., Rocha, N., Mommaas, M., Huizing, M., Lambert, J., Naeyaert, J. M., & Neefjes, J. (2006) · Pigment Cell Research · doi:10.1111/j.1600-0749.2006.00329.x · Cited by 98
Hume, A. N., Tarafder, A. K., Ramalho, J. S., Sviderskaya, E. V., & Seabra, M. C. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0457 · Cited by 91
Self-citationAction and interactions at microtubule ends
Morrison, E. E. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6360-3 · Cited by 90
Barth, A. I. M., Siemers, K. A., & Nelson, W. J. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1583 · Cited by 86
Role of Cytoplasmic Dynein in Melanosome Transport in Human Melanocytes
Byers, H. R., Yaar, M., Eller, M. S., Jalbert, N. L., & Gilchrest, B. A. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00957.x · Cited by 80
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
Regulation of Cutaneous Allergic Reaction by Odorant Inhalation
Hosoi, J., & Tsuchiya, T. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00896.x · Cited by 62
Vancoillie, G., Lambert, J., Naeyaert, J. M., Mulder, A. A., Koerten, H. K., Mommaas, A. M., & Oostveldt, P. V. (2000) · Journal of Investigative Dermatology · doi:10.1038/jid.2000.3 · Cited by 47
Cytoplasmic dynein colocalizes with melanosomes in normal human melanocytes
Vancoillie, G., Lambert, J., Mulder, A. A., Koerten, H. K., Mommaas, A. M., Oostveldt, P. V., & Naeyaert, J. M. (2000) · British Journal of Dermatology · doi:10.1046/j.1365-2133.2000.03654.x · Cited by 39
Vancoillie, G., Lambert, J., Mulder, A. A., et al. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00897.x · Cited by 14
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Cieslak, M., Reißmann, M., Hofreiter, M., & Ludwig, A. (2011) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2011.00177.x · Cited by 283
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Chiavérini, C., Beuret, L., Flori, E., Buscà, R., Abbe, P., Bille, K., Bahadoran, P., Ortonne, J. P., Bertolotto, C., & Ballotti, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800130200 · Cited by 120
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Aspengren, S., Hedberg, D., Sköld, H. N., & Wallin, M. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01606-7 · Cited by 125
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Billaud, M., Lohman, A. W., Johnstone, S. R., Biwer, L. A., Mutchler, S. M., & Isakson, B. E. (2014) · Pharmacological Reviews · doi:10.1124/pr.112.007351 · Cited by 116
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“At the cell periphery, melanosomes are anchored to the cortical actin network and unidirectionally transported to the plasma membrane by the tripartite complex composed of the secretory protein Rab27a, the adaptor protein melanophilin, and the actin-dependent motor protein myosin Va [40,41] (Figure 3A).”
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Rab11‐ FIP2 Interaction with MYO5B Regulates Movement of Rab11a‐Containing Recycling Vesicles
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Figueiredo, A. C., Wasmeier, C., Tarafder, A. K., Ramalho, J. S., Baron, R., & Seabra, M. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804134200 · Cited by 65
Self-citationThe Tail that Wags the Dog: The Globular Tail Domain Defines the Function of Myosin V/XI
Li, J., & Nebenführ, A. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00687.x · Cited by 63
Alzahofi, N., Welz, T., Robinson, C. L., Page, E. L., Briggs, D. A., Stainthorp, A. K., Reekes, J., Elbe, D. A., Straub, F., Kallemeijn, W. W., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17212-6 · Cited by 61
Self-citationHerráiz, C., Martínez‐Vicente, I., & Maresca, V. (2021) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12980 · Cited by 65
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Self-citationLi, D., Wang, X., Fu, Y., Zhang, C., Cao, Y., Wang, J., Zhang, Y., Li, Y., Chen, Y., Li, Z., et al. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00457 · Cited by 41
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Sun, X. Y., He, Y., Hou, L., & Yang, W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012738 · Cited by 36
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Miao, Y., Bist, P., Wu, J., Zhao, Q., Li, Q., Wan, Y., & Abraham, S. N. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.08.002 · Cited by 36
Yu, S., Wang, G., Liao, J., & Tang, M. (2018) · Poultry Science · doi:10.3382/ps/pey238 · Cited by 35
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Chen, S., Guo, X., He, X., Di, R., Zhang, X., Zhang, J., Wang, X., & Chu, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.633747 · Cited by 26
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Self-citation
Metadata
- Authors
- Hume, A. N., Ushakov, D. S., Tarafder, A. K., Ferenczi, M. A., & Seabra, M. C.
- Affiliations
- Imperial College London (GB)
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2007-09-01
- Volume
- 120
- Issue
- 17
- Pages
- 3111-3122
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2074266972
- Cited by
- 103
- References
- 41
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 10 · 2020: 6 · 2019: 10 · 2018: 3 · 2017: 3 · 2016: 2 · 2015: 1 · 2014: 6 · 2013: 4 · 2012: 4
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- other-oa
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (075498)
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- melanosome transport, melanocytes, melanophilin, Rab27a, myosin Va, EB1, protein-protein interaction, actin-based transport, melanosomes
- MeSH terms
- rab27 GTP-Binding Proteins, Amino Acid Sequence, Animals, Binding Sites, Biological Transport, Humans, Melanocytes, Microtubule-Associated Proteins, Molecular Sequence Data, Protein Binding, Sequence Alignment, Myosin Heavy Chains, Melanosomes, rab GTP-Binding Proteins, Two-Hybrid System Techniques, Myosin Type V, RNA, Small Interfering, Adaptor Proteins, Signal Transducing, Mice
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