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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 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]
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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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