ArticleThe Journal of biological chemistry2013
More than just a cargo adapter, melanophilin prolongs and slows processive runs of myosin Va.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- Cargo Recognition of Nesprin-2 by the Dynein Adapter Bicaudal D2 for a Nuclear Positioning Pathway That Is Important for Brain Development.Biochemistry · 2026Article
- Cross-tissue transcriptome-wide association studies identify genetic susceptibility genes for prostate cancer.BMC cancer · 2025Article
- Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing.Nature communications · 2025Article
- Article
- The type V myosin-containing complex HUM is a RAB11 effector powering movement of secretory vesicles.iScience · 2022Article
- Coil-to-α-helix transition at the Nup358-BicD2 interface activates BicD2 for dynein recruitment.eLife · 2022Article
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- Evolutionary selection of alleles in the melanophilin gene that impacts on prostate organ function and cancer risk.Evolution, medicine, and public health · 2021Article
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Molecular underpinnings of cytoskeletal cross-talk.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- The cargo adaptor proteins RILPL2 and melanophilin co-regulate myosin-5a motor activity.The Journal of biological chemistry · 2019Article
- Myosin-Driven Intracellular Transport.Cold Spring Harbor perspectives in biology · 2018Review
- 36H: A Novel Potent Inhibitor for Antimelanogenesis.Oxidative medicine and cellular longevity · 2018Article
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Myosin Va's adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Calmodulin in complex with the first IQ motif of myosin-5a functions as an intact calcium sensor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Tropomyosin isoforms bias actin track selection by vertebrate myosin Va.Molecular biology of the cell · 2016Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosin Va (myoVa) is a molecular motor that processively transports cargo along actin tracks. One well studied cargo in vivo is the melanosome, a pigment organelle that is moved first by kinesin on microtubules and then handed off to myoVa for transport in the actin-rich dendritic periphery of melanocytes. Melanophilin (Mlph) is the adapter protein that links Rab27a-melanosomes to myoVa. Using total internal reflection fluorescence microscopy and quantum dot-labeled full-length myoVa, we show at the single-molecule level that Mlph increases the number of processively moving myoVa motors by 17-fold. Surprisingly, myoVa-Mlph moves ~4-fold slower than myoVa alone and with twice the run length. These two changes greatly increase the time spent on actin, a property likely to enhance the transfer of melanosomes to the adjacent keratinocyte. In contrast to the variable stepping pattern of full-length myoVa, the myoVa-Mlph complex shows a normal gating pattern between the heads typical of a fully active motor and consistent with a cargo-dependent activation mechanism. The Mlph-dependent changes in myoVa depend on a positively charged cluster of amino acids in the actin binding domain of Mlph, suggesting that Mlph acts as a "tether" that links the motor to the track. Our results provide a molecular explanation for the uncharacteristically slow speed of melanosome movement by myoVa in vivo. More generally, these data show that proteins that link motors to cargo can modify motor properties to enhance their biological role.
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