ArticleMolecular and cellular biology2003
The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49 citing papers in PubMed, 121 citations in OpenAlex.
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- AID-2×RBD27, an auxin-inducible degron-based Rab27 trapper that reversibly inhibits the function of Rab27A in melanocytes.Journal of cell science · 2025Article
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- Rab32/38-Dependent and -Independent Transport of Tyrosinase to Melanosomes in B16-F1 Melanoma Cells.International journal of molecular sciences · 2022Article
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- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Whitening effect of novel peptide mixture by regulating melanosome biogenesis, transfer and degradation.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2021Article
- Molecular underpinnings of cytoskeletal cross-talk.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Griscelli Syndrome Type 2 Sine Albinism: Unraveling Differential RAB27A Effector Engagement.Frontiers in immunology · 2020Article
- Insights Into the Albinism Mechanism for Two Distinct Color Morphs of Northern Snakehead,Frontiers in genetics · 2020Article
- A novel function of Prohibitin on melanosome transport in melanocytes.Theranostics · 2020Article
- Knockdown of microRNA‑143‑5p by STTM technology affects eumelanin and pheomelanin production in melanocytes.Molecular medicine reports · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Melanosomes containing melanin pigments are transported from the cell body of melanocytes to the tips of their dendrites by a combination of microtubule- and actin-dependent machinery. Three proteins, Rab27A, myosin Va, and Slac2-a/melanophilin (a linker protein between Rab27A and myosin Va), are known to be essential for proper actin-based melanosome transport in melanocytes. Although Slac2-a directly interacts with Rab27A and myosin Va via its N-terminal region (amino acids 1 to 146) and the middle region (amino acids 241 to 405), respectively, the functional importance of the putative actin-binding domain of the Slac2-a C terminus (amino acids 401 to 590) in melanosome transport has never been elucidated. In this study we showed that formation of a tripartite protein complex between Rab27A, Slac2-a, and myosin Va alone is insufficient for peripheral distribution of melanosomes in melanocytes and that the C-terminal actin-binding domain of Slac2-a is also required for proper melanosome transport. When a Slac2-a deletion mutant (DeltaABD) or point mutant (KA) that lacks actin-binding ability was expressed in melanocytes, the Slac2-a mutants induced melanosome accumulation in the perinuclear region, possibly by a dominant negative effect, the same as the Rab27A-binding-defective mutant of Slac2-a or the myosin Va-binding-defective mutant. Our findings indicate that Slac2-a organizes actin-based melanosome transport in cooperation with Rab27A, myosin Va, and actin.
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