ArticleMolecular biology of the cell1997
Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 90 citations in OpenAlex.
- Altered mitochondrial trafficking as a novel mechanism of cancer metastasis.Cancer reports (Hoboken, N.J.) · 2020Review
- Duplicated Myosin V Genes in Teleosts Show Evolutionary Rate Variations among the Motor and Cargo-Binding Domains.Genome biology and evolution · 2019Article
- Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.Biophysical journal · 2016Article
- Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural basis of cargo recognitions for class V myosins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Myosin Va is developmentally regulated and expressed in the human cerebellum from birth to old age.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2013Article
- Rab GTPases implicated in inherited and acquired disorders.Seminars in cell & developmental biology · 2011Review
- Article
- Human myosin Vc is a low duty ratio nonprocessive motor.The Journal of biological chemistry · 2008Article
- The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae.The Journal of cell biology · 2008Article
- Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells.Molecular biology of the cell · 2005Article
- A point mutation in the cargo-binding domain of myosin V affects its interaction with multiple cargoes.Eukaryotic cell · 2005Article
- Myosin V attachment to cargo requires the tight association of two functional subdomains.The Journal of cell biology · 2005Article
- Intracellular actin-based transport: how far you go depends on how often you switch.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Myosin-Va binds to and mechanochemically couples microtubules to actin filaments.Molecular biology of the cell · 2004Article
- The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes.Molecular and cellular biology · 2003Article
- Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport.Molecular biology of the cell · 2003Article
- Rab27a is an essential component of melanosome receptor for myosin Va.Molecular biology of the cell · 2002Article
- Myosin Va bound to phagosomes binds to F-actin and delays microtubule-dependent motility.Molecular biology of the cell · 2001Article
- Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The discovery that the dilute gene encodes a class V myosin led to the hypothesis that this molecular motor is involved in melanosome transport and/or dendrite outgrowth in mammalian melanocytes. The present studies were undertaken to gain insight into the subcellular distribution of myosin-V in the melanoma cell line B16-F10, which is wild-type for the dilute gene. Immunofluorescence studies showed some degree of superimposed labeling of myosin-V with melanosomes that predominated at the cell periphery. A subcellular fraction highly enriched in melanosomes was also enriched in myosin-V based on Western blot analysis. Immunoelectron microscopy showed myosin-V labeling associated with melanosomes and other organelles. The stimulation of B16 cells with the alpha-melanocyte-stimulating hormone led to a significant increase in myosin-V expression. This is the first evidence that a cAMP signaling pathway might regulate the dilute gene expression. Immunofluorescence also showed an intense labeling of myosin-V independent of melanosomes that was observed within the dendrites and at the perinuclear region. Although the results presented herein are consistent with the hypothesis that myosin-V might act as a motor for melanosome translocation, they also suggest a broader cytoplasmic function for myosin-V, acting on other types of organelles or in cytoskeletal dynamics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.