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Journal articles on the topic 'Melanosomy'

Author: Grafiati

Published: 24 April 2022

Last updated: 30 July 2025

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1

Futter, Clare E., and Daniel F. Cutler. "Coming or going? Un-BLOC-ing delivery and recycling pathways during melanosome maturation." Journal of Cell Biology 214, no. 3 (2016): 245–47. http://dx.doi.org/10.1083/jcb.201607023.

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Melanosome biogenesis requires successive waves of cargo delivery from endosomes to immature melanosomes, coupled with recycling of the trafficking machinery. Dennis et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201605090) report differential roles for BLOC-1 and BLOC-3 complexes in delivery and recycling of melanosomal biogenetic components, supplying directionality to melanosome maturation.

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2

Hume, Alistair N., Abul K. Tarafder, José S. Ramalho, Elena V. Sviderskaya, and Miguel C. Seabra. "A Coiled-Coil Domain of Melanophilin Is Essential for Myosin Va Recruitment and Melanosome Transport in Melanocytes." Molecular Biology of the Cell 17, no. 11 (2006): 4720–35. http://dx.doi.org/10.1091/mbc.e06-05-0457.

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Melanophilin (Mlph) regulates retention of melanosomes at the peripheral actin cytoskeleton of melanocytes, a process essential for normal mammalian pigmentation. Mlph is proposed to be a modular protein binding the melanosome-associated protein Rab27a, Myosin Va (MyoVa), actin, and microtubule end-binding protein (EB1), via distinct N-terminal Rab27a-binding domain (R27BD), medial MyoVa-binding domain (MBD), and C-terminal actin-binding domain (ABD), respectively. We developed a novel melanosome transport assay using a Mlph-null cell line to study formation of the active Rab27a:Mlph:MyoVa com

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Ohbayashi, Norihiko, and Mitsunori Fukuda. "Recent advances in understanding the molecular basis of melanogenesis in melanocytes." F1000Research 9 (June 15, 2020): 608. http://dx.doi.org/10.12688/f1000research.24625.1.

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Melanin pigments are responsible for human skin and hair color, and they protect the body from harmful ultraviolet light. The black and brown melanin pigments are synthesized in specialized lysosome-related organelles called melanosomes in melanocytes. Mature melanosomes are transported within melanocytes and transferred to adjacent keratinocytes, which constitute the principal part of human skin. The melanosomes are then deposited inside the keratinocytes and darken the skin (a process called tanning). Owing to their dark color, melanosomes can be seen easily with an ordinary light microscope

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4

Sitaram, Anand, Megan K. Dennis, Rittik Chaudhuri, et al. "Differential recognition of a dileucine-based sorting signal by AP-1 and AP-3 reveals a requirement for both BLOC-1 and AP-3 in delivery of OCA2 to melanosomes." Molecular Biology of the Cell 23, no. 16 (2012): 3178–92. http://dx.doi.org/10.1091/mbc.e11-06-0509.

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Cell types that generate unique lysosome-related organelles (LROs), such as melanosomes in melanocytes, populate nascent LROs with cargoes that are diverted from endosomes. Cargo sorting toward melanosomes correlates with binding via cytoplasmically exposed sorting signals to either heterotetrameric adaptor AP-1 or AP-3. Some cargoes bind both adaptors, but the relative contribution of each adaptor to cargo recognition and their functional interactions with other effectors during transport to melanosomes are not clear. Here we exploit targeted mutagenesis of the acidic dileucine–based sorting

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5

Robinson, Christopher L., Richard D. Evans, Kajana Sivarasa, Jose S. Ramalho, Deborah A. Briggs, and Alistair N. Hume. "The adaptor protein melanophilin regulates dynamic myosin-Va:cargo interaction and dendrite development in melanocytes." Molecular Biology of the Cell 30, no. 6 (2019): 742–52. http://dx.doi.org/10.1091/mbc.e18-04-0237.

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The regulation of organelle transport by the cytoskeleton is fundamental for eukaryotic survival. Cytoskeleton motors are typically modular proteins with conserved motor and diverse cargo-binding domains. Motor:cargo interactions are often indirect and mediated by adaptor proteins, for example, Rab GTPases. Rab27a, via effector melanophilin (Mlph), recruits myosin-Va (MyoVa) to melanosomes and thereby disperses them into melanocyte dendrites. To better understand how adaptors regulate motor:cargo interaction, we used single melanosome fluorescence recovery after photobleaching (smFRAP) to char

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Setty, Subba Rao Gangi, Danièle Tenza, Steven T. Truschel, et al. "BLOC-1 Is Required for Cargo-specific Sorting from Vacuolar Early Endosomes toward Lysosome-related Organelles." Molecular Biology of the Cell 18, no. 3 (2007): 768–80. http://dx.doi.org/10.1091/mbc.e06-12-1066.

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Hermansky-Pudlak syndrome (HPS) is a genetic disorder characterized by defects in the formation and function of lysosome-related organelles such as melanosomes. HPS in humans or mice is caused by mutations in any of 15 genes, five of which encode subunits of biogenesis of lysosome-related organelles complex (BLOC)-1, a protein complex with no known function. Here, we show that BLOC-1 functions in selective cargo exit from early endosomes toward melanosomes. BLOC-1–deficient melanocytes accumulate the melanosomal protein tyrosinase-related protein-1 (Tyrp1), but not other melanosomal proteins,

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Ambrosio, Andrea L., Judith A. Boyle, Al E. Aradi, Keith A. Christian, and Santiago M. Di Pietro. "TPC2 controls pigmentation by regulating melanosome pH and size." Proceedings of the National Academy of Sciences 113, no. 20 (2016): 5622–27. http://dx.doi.org/10.1073/pnas.1600108113.

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Melanin is responsible for pigmentation of skin and hair and is synthesized in a specialized organelle, the melanosome, in melanocytes. A genome-wide association study revealed that the two pore segment channel 2 (TPCN2) gene is strongly linked to pigmentation variations. TPCN2 encodes the two-pore channel 2 (TPC2) protein, a cation channel. Nevertheless, how TPC2 regulates pigmentation remains unknown. Here, we show that TPC2 is expressed in melanocytes and localizes to the melanosome-limiting membrane and, to a lesser extent, to endolysosomal compartments by confocal fluorescence and immunog

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8

Wan, Jiyue, Shumiao Zhang, Guiling Li, et al. "Ceramide Ehux-C22 Targets the miR-199a-3p/mTOR Signaling Pathway to Regulate Melanosomal Autophagy in Mouse B16 Cells." International Journal of Molecular Sciences 25, no. 15 (2024): 8061. http://dx.doi.org/10.3390/ijms25158061.

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Melanosomes are specialized membrane-bound organelles where melanin is synthesized and stored. The levels of melanin can be effectively reduced by inhibiting melanin synthesis or promoting melanosome degradation via autophagy. Ceramide, a key component in the metabolism of sphingolipids, is crucial for preserving the skin barrier, keeping it hydrated, and warding off the signs of aging. Our preliminary study indicated that a long-chain C22-ceramide compound (Ehux-C22) isolated from the marine microalga Emiliania huxleyi, reduced melanin levels via melanosomal autophagy in B16 cells. Recently,

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Delevoye, Cédric, Ilse Hurbain, Danièle Tenza, et al. "AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis." Journal of Cell Biology 187, no. 2 (2009): 247–64. http://dx.doi.org/10.1083/jcb.200907122.

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Specialized cell types exploit endosomal trafficking to deliver protein cargoes to cell type–specific lysosome-related organelles (LROs), but how endosomes are specified for this function is not known. In this study, we show that the clathrin adaptor AP-1 and the kinesin motor KIF13A together create peripheral recycling endosomal subdomains in melanocytes required for cargo delivery to maturing melanosomes. In cells depleted of AP-1 or KIF13A, a subpopulation of recycling endosomes redistributes to pericentriolar clusters, resulting in sequestration of melanosomal enzymes like Tyrp1 in vacuola

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10

Rogers, Christopher S., Timothy I. Astrop, Samuel M. Webb, Shosuke Ito, Kazumasa Wakamatsu, and Maria E. McNamara. "Synchrotron X-ray absorption spectroscopy of melanosomes in vertebrates and cephalopods: implications for the affinity of Tullimonstrum." Proceedings of the Royal Society B: Biological Sciences 286, no. 1913 (2019): 20191649. http://dx.doi.org/10.1098/rspb.2019.1649.

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Screening pigments are essential for vision in animals. Vertebrates use melanins bound in melanosomes as screening pigments, whereas cephalopods are assumed to use ommochromes. Preserved eye melanosomes in the controversial fossil Tullimonstrum (Mazon Creek, IL, USA) are partitioned by size and/or shape into distinct layers. These layers resemble tissue-specific melanosome populations considered unique to the vertebrate eye. Here, we show that extant cephalopod eyes also show tissue-specific size- and/or shape-specific partitioning of melanosomes; these differ from vertebrate melanosomes in th

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Hida, Tokimasa, Takafumi Kamiya, Akinori Kawakami, et al. "Elucidation of Melanogenesis Cascade for Identifying Pathophysiology and Therapeutic Approach of Pigmentary Disorders and Melanoma." International Journal of Molecular Sciences 21, no. 17 (2020): 6129. http://dx.doi.org/10.3390/ijms21176129.

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Melanogenesis is the biological and biochemical process of melanin and melanosome biosynthesis. Melanin is formed by enzymic reactions of tyrosinase family proteins that convert tyrosine to form brown-black eumelanin and yellow-red pheomelanin within melanosomal compartments in melanocytes, following the cascades of events interacting with a series of autocrine and paracrine signals. Fully melanized melanosomes are delivered to keratinocytes of the skin and hair. The symbiotic relation of a melanocyte and an associated pool of keratinocytes is called epidermal melanin unit (EMU). Microphthalmi

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Ohbayashi, Norihiko, and Mitsunori Fukuda. "SNARE dynamics during melanosome maturation." Biochemical Society Transactions 46, no. 4 (2018): 911–17. http://dx.doi.org/10.1042/bst20180130.

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Historically, studies on the maturation and intracellular transport of melanosomes in melanocytes have greatly contributed to elucidating the general mechanisms of intracellular transport in many different types of mammalian cells. During melanosome maturation, melanosome cargoes including melanogenic enzymes (e.g. tyrosinase) are transported from endosomes to immature melanosomes by membrane trafficking, which must require a membrane fusion process likely regulated by SNAREs [soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors]. In the present study, we review the lit

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Lopes, Vanda S., Christina Wasmeier, Miguel C. Seabra, and Clare E. Futter. "Melanosome Maturation Defect in Rab38-deficient Retinal Pigment Epithelium Results in Instability of Immature Melanosomes during Transient Melanogenesis." Molecular Biology of the Cell 18, no. 10 (2007): 3914–27. http://dx.doi.org/10.1091/mbc.e07-03-0268.

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Pathways of melanosome biogenesis in retinal pigment epithelial (RPE) cells have received less attention than those of skin melanocytes. Although the bulk of melanin synthesis in RPE cells occurs embryonically, it is not clear whether adult RPE cells continue to produce melanosomes. Here, we show that progression from pmel17-positive premelanosomes to tyrosinase-positive mature melanosomes in the RPE is largely complete before birth. Loss of functional Rab38 in the “chocolate” (cht) mouse causes dramatically reduced numbers of melanosomes in adult RPE, in contrast to the mild phenotype previou

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Ripoll, Léa, Xavier Heiligenstein, Ilse Hurbain, et al. "Myosin VI and branched actin filaments mediate membrane constriction and fission of melanosomal tubule carriers." Journal of Cell Biology 217, no. 8 (2018): 2709–26. http://dx.doi.org/10.1083/jcb.201709055.

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Vesicular and tubular transport intermediates regulate organellar cargo dynamics. Transport carrier release involves local and profound membrane remodeling before fission. Pinching the neck of a budding tubule or vesicle requires mechanical forces, likely exerted by the action of molecular motors on the cytoskeleton. Here, we show that myosin VI, together with branched actin filaments, constricts the membrane of tubular carriers that are then released from melanosomes, the pigment containing lysosome-related organelles of melanocytes. By combining superresolution fluorescence microscopy, corre

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15

Wang, Siqun, Shirley Bartido, George Yang, et al. "A Role for a Melanosome Transport Signal in Accessing the MHC Class II Presentation Pathway and in Eliciting CD4+ T Cell Responses." Journal of Immunology 163, no. 11 (1999): 5820–26. http://dx.doi.org/10.4049/jimmunol.163.11.5820.

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Abstract Melanosomal membrane proteins are frequently recognized by the immune system of patients with melanoma and vitiligo. Melanosomal glycoproteins are transported to melanosomes by a dileucine-based melanosomal transport signal (MTS). To investigate whether this sorting signal could be involved in presentation of melanosome membrane proteins to the immune system, we devised a fusion construct containing the MTS from the mouse brown locus product gp75/tyrosinase-related protein-1 and full-length OVA as a reporter Ag. The fusion protein was expressed as an intracellular membrane protein, so

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Scott, Glynis, Sonya Leopardi, Stacey Printup, and Brian C. Madden. "Filopodia are conduits for melanosome transfer to keratinocytes." Journal of Cell Science 115, no. 7 (2002): 1441–51. http://dx.doi.org/10.1242/jcs.115.7.1441.

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Melanosomes are specialized melanin-synthesizing organelles critical for photoprotection in the skin. Melanosome transfer to keratinocytes, which involves whole organelle donation to another cell, is a unique biological process and is poorly understood. Time-lapse digital movies and electron microscopy show that filopodia from melanocyte dendrites serve as conduits for melanosome transfer to keratinocytes. Cdc42, a small GTP-binding protein, is known to mediate filopodia formation. Melanosome-enriched fractions isolated from human melanocytes expressed the Cdc42 effector proteins PAK1 and N-WA

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Bartosik, J. "Melanosome complexes and melanin macroglobules in normal human skin." Acta Dermato-Venereologica 71, no. 4 (1991): 283–86. http://dx.doi.org/10.2340/0001555571283286.

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The presence of melanin macroglobules, and sometimes that of melanosome complexes also, in epidermal melanocytes has been considered a feature of various skin diseases. Opinions differ as to whether these structures can occur in normal skin. We have studied these melanin inclusions in normal Caucasian skin in the entire soma of 116 melanocytes and the occurrence of melanosomes in phagosomes of 77 Langerhans' cells obtained in different seasons. During winter the melanocytes contained few melanosomes but many melanosome complexes and melanin macroglobules. These melanosome inclusions were in 86

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Wu, X., K. Rao, M. B. Bowers, N. G. Copeland, N. A. Jenkins, and J. A. Hammer. "Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle." Journal of Cell Science 114, no. 6 (2001): 1091–100. http://dx.doi.org/10.1242/jcs.114.6.1091.

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The peripheral accumulation of melanosomes characteristic of wild-type mouse melanocytes is driven by a cooperative process involving long-range, bidirectional, microtubule-dependent movements coupled to capture and local movement in the actin-rich periphery by myosin Va, the product of the dilute locus. Genetic evidence suggests that Rab27a, the product of the ashen locus, functions with myosin Va in this process. Here we show that ashen melanocytes, like dilute melanocytes, exhibit normal dendritic morphology and melanosome biogenesis, an abnormal accumulation of end-stage melanosomes in the

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Wu, Xufeng, Blair Bowers, Kang Rao, Qin Wei, and John A. Hammer. "Visualization of Melanosome Dynamics within Wild-Type and Dilute Melanocytes Suggests a Paradigm for Myosin V Function In Vivo." Journal of Cell Biology 143, no. 7 (1998): 1899–918. http://dx.doi.org/10.1083/jcb.143.7.1899.

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Unlike wild-type mouse melanocytes, where melanosomes are concentrated in dendrites and dendritic tips, melanosomes in dilute (myosin Va−) melanocytes are concentrated in the cell center. Here we sought to define the role that myosin Va plays in melanosome transport and distribution. Actin filaments that comprise a cortical shell running the length of the dendrite were found to exhibit a random orientation, suggesting that myosin Va could drive the outward spreading of melanosomes by catalyzing random walks. In contrast to this mechanism, time lapse video microscopy revealed that melanosomes u

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Andreola, Giovanna, Licia Rivoltini, Chiara Castelli, et al. "Induction of Lymphocyte Apoptosis by Tumor Cell Secretion of FasL-bearing Microvesicles." Journal of Experimental Medicine 195, no. 10 (2002): 1303–16. http://dx.doi.org/10.1084/jem.20011624.

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The hypothesis that FasL expression by tumor cells may impair the in vivo efficacy of antitumor immune responses, through a mechanism known as ‘Fas tumor counterattack,’ has been recently questioned, becoming the object of an intense debate based on conflicting results. Here we definitely show that FasL is indeed detectable in the cytoplasm of melanoma cells and its expression is confined to multivesicular bodies that contain melanosomes. In these structures FasL colocalizes with both melanosomal (i.e., gp100) and lysosomal (i.e., CD63) antigens. Isolated melanosomes express FasL, as detected

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Wu, X., B. Bowers, Q. Wei, B. Kocher, and J. A. Hammer. "Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor." Journal of Cell Science 110, no. 7 (1997): 847–59. http://dx.doi.org/10.1242/jcs.110.7.847.

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Mice with mutations at the dilute locus exhibit a ‘washed out’ or ‘diluted’ coat color. The pigments that are responsible for the coloration of mammalian hair are produced by melanocytes within a specialized organelle, the melanosome. Each melanocyte is responsible for delivering melanosomes via its extensive dendritic arbor to numerous keratinocytes, which go on to form the pigmented hair shaft. In this study, we show by light immunofluorescence microscopy and immunoelectron microscopy that the myosin V isoform encoded by the dilute locus associates with melanosomes. This association, which w

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KING-SMITH, CHRISTINA, RONALD J. VAGNOZZI, NICOLE E. FISCHER, PATRICK GANNON, and SATYA GUNNAM. "Orientation of actin filaments in teleost retinal pigment epithelial cells, and the effect of the lectin, Concanavalin A, on melanosome motility." Visual Neuroscience 31, no. 1 (2014): 1–10. http://dx.doi.org/10.1017/s0952523813000618.

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AbstractRetinal pigment epithelial cells of teleosts contain numerous melanosomes (pigment granules) that exhibit light-dependent motility. In light, melanosomes disperse out of the retinal pigment epithelium (RPE) cell body (CB) into long apical projections that interdigitate with rod photoreceptors, thus shielding the photoreceptors from bleaching. In darkness, melanosomes aggregate through the apical projections back into the CB. Previous research has demonstrated that melanosome motility in the RPE CB requires microtubules, but in the RPE apical projections, actin filaments are necessary a

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Wu, Xufeng, Fei Wang, Kang Rao, James R. Sellers, and John A. Hammer. "Rab27a Is an Essential Component of Melanosome Receptor for Myosin Va." Molecular Biology of the Cell 13, no. 5 (2002): 1735–49. http://dx.doi.org/10.1091/mbc.01-12-0595.

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Melanocytes that lack the GTPase Rab27a (ashen) are disabled in myosin Va-dependent melanosome capture because the association of the myosin with the melanosome surface depends on the presence of this resident melanosomal membrane protein. One interpretation of these observations is that Rab27a functions wholly or in part as the melanosome receptor for myosin Va (Myo5a). Herein, we show that the ability of the myosin Va tail domain to localize to the melanosome and generate a myosin Va null (dilute) phenotype in wild-type melanocytes is absolutely dependent on the presence of exon F, one of tw

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Bahadoran, Philippe, Edith Aberdam, Frédéric Mantoux, et al. "Rab27a." Journal of Cell Biology 152, no. 4 (2001): 843–50. http://dx.doi.org/10.1083/jcb.152.4.843.

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Normal pigmentation depends on the uniform distribution of melanin-containing vesicles, the melanosomes, in the epidermis. Griscelli syndrome (GS) is a rare autosomal recessive disease, characterized by an immune deficiency and a partial albinism that has been ascribed to an abnormal melanosome distribution. GS maps to 15q21 and was first associated with mutations in the myosin-V gene. However, it was demonstrated recently that GS can also be caused by a mutation in the Rab27a gene. These observations prompted us to investigate the role of Rab27a in melanosome transport. Using immunofluorescen

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McNamara, Maria E., Derek E. G. Briggs, Patrick J. Orr, Daniel J. Field, and Zhengrong Wang. "Experimental maturation of feathers: implications for reconstructions of fossil feather colour." Biology Letters 9, no. 3 (2013): 20130184. http://dx.doi.org/10.1098/rsbl.2013.0184.

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Fossil feathers often preserve evidence of melanosomes—micrometre-scale melanin-bearing organelles that have been used to infer original colours and patterns of the plumage of dinosaurs. Such reconstructions acknowledge that evidence from other colour-producing mechanisms is presently elusive and assume that melanosome geometry is not altered during fossilization. Here, we provide the first test of this assumption, using high pressure–high temperature autoclave experiments on modern feathers to simulate the effects of burial on feather colour. Our experiments show that melanosomes are retained

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Lee, Jeong Ah, Seok Joon Hwang, Sung Chan Hong, et al. "Identification of MicroRNA Targeting Mlph and Affecting Melanosome Transport." Biomolecules 9, no. 7 (2019): 265. http://dx.doi.org/10.3390/biom9070265.

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Melanosomes undergo a complex maturation process and migrate into keratinocytes. Melanophilin (Mlph), a protein complex involving myosin Va (MyoVa) and Rab27a, enables the movement of melanosomes in melanocytes. In this study, we found six miRNAs targeting Mlph in mouse using two programs (http://targetscan.org and DianaTools). When melan-a melanocytes were treated with six synthesized microRNAs, miR-342-5p, miR-1839-5p, and miR-3082-5p inhibited melanosome transport and induced melanosome aggregation around the nucleus. The other microRNAs, miR-5110, miR-3090-3p, and miR-186-5p, did not inhib

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Futter, Clare E., José S. Ramalho, Gesine B. Jaissle, Mathias W. Seeliger, and Miguel C. Seabra. "The Role of Rab27a in the Regulation of Melanosome Distribution within Retinal Pigment Epithelial Cells." Molecular Biology of the Cell 15, no. 5 (2004): 2264–75. http://dx.doi.org/10.1091/mbc.e03-10-0772.

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Melanosomes within the retinal pigment epithelium (RPE) of mammals have long been thought to exhibit no movement in response to light, unlike fish and amphibian RPE. Here we show that the distribution of melanosomes within the mouse RPE undergoes modest but significant changes with the light cycle. Two hours after light onset, there is a threefold increase in the number of melanosomes in the apical processes that surround adjacent photoreceptors. In skin melanocytes, melanosomes are motile and evenly distributed throughout the cell periphery. This distribution is due to the interaction with th

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Babarović, Frane, Mark N. Puttick, Marta Zaher, et al. "Characterization of melanosomes involved in the production of non-iridescent structural feather colours and their detection in the fossil record." Journal of The Royal Society Interface 16, no. 155 (2019): 20180921. http://dx.doi.org/10.1098/rsif.2018.0921.

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Non-iridescent structural colour in avian feathers is produced by coherent light scattering through quasi-ordered nanocavities in the keratin cortex of the barbs. To absorb unscattered light, melanosomes form a basal layer underneath the nanocavities. It has been shown that throughout Aves, melanosome morphology reflects broad categories of melanin-based coloration, as well as iridescence, allowing identification of palaeocolours in exceptionally preserved fossils. However, no studies have yet investigated the morphology of melanosomes in non-iridescent structural colour. Here, we analyse a wi

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D’Alba, Liliana, and Matthew D. Shawkey. "Melanosomes: Biogenesis, Properties, and Evolution of an Ancient Organelle." Physiological Reviews 99, no. 1 (2019): 1–19. http://dx.doi.org/10.1152/physrev.00059.2017.

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Melanosomes are organelles that produce and store melanin, a widespread biological pigment with a unique suite of properties including high refractive index, semiconducting capabilities, material stiffness, and high fossilization potential. They are involved in numerous critical biological functions in organisms across the tree of life. Individual components such as melanin chemistry and melanosome development have recently been addressed, but a broad synthesis is needed. Here, we review the hierarchical structure, development, functions, and evolution of melanosomes. We highlight variation in

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Theos, Alexander C., Danièle Tenza, José A. Martina, et al. "Functions of Adaptor Protein (AP)-3 and AP-1 in Tyrosinase Sorting from Endosomes to Melanosomes." Molecular Biology of the Cell 16, no. 11 (2005): 5356–72. http://dx.doi.org/10.1091/mbc.e05-07-0626.

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Specialized cells exploit adaptor protein complexes for unique post-Golgi sorting events, providing a unique model system to specify adaptor function. Here, we show that AP-3 and AP-1 function independently in sorting of the melanocyte-specific protein tyrosinase from endosomes to the melanosome, a specialized lysosome-related organelle distinguishable from lysosomes. AP-3 and AP-1 localize in melanocytes primarily to clathrin-coated buds on tubular early endosomes near melanosomes. Both adaptors recognize the tyrosinase dileucine-based melanosome sorting signal, and tyrosinase largely colocal

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Eliason, Chad M., Pierre-Paul Bitton, and Matthew D. Shawkey. "How hollow melanosomes affect iridescent colour production in birds." Proceedings of the Royal Society B: Biological Sciences 280, no. 1767 (2013): 20131505. http://dx.doi.org/10.1098/rspb.2013.1505.

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Developmental constraints and trade-offs can limit diversity, but organisms have repeatedly evolved morphological innovations that overcome these limits by expanding the range and functionality of traits. Iridescent colours in birds are commonly produced by melanin-containing organelles (melanosomes) organized into nanostructured arrays within feather barbules. Variation in array type (e.g. multilayers and photonic crystals, PCs) is known to have remarkable effects on plumage colour, but the optical consequences of variation in melanosome shape remain poorly understood. Here, we used a combina

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Wang, Jiafeng, and Bin Chen. "Bubble Dynamics during Laser Irradiated Thermo-Mechanical Response of Pigmented Skin Phantom." Energies 15, no. 6 (2022): 2019. http://dx.doi.org/10.3390/en15062019.

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During the laser treatment of pigmented dermatosis such as Nevus of Ota, vapor bubbles will be generated by the laser with short pulse width and high energy density. Laser irradiation is efficacious for the clinical treatment of Ota’s Nevus caused by hyperplasia of melanosomes in dermis. Since the mechanism of the laser–melanosome interaction is not yet clear, the clearance rate is generally low and bleeding of irradiated skin frequently occurs. This work conducted a flow visualization experiment to investigate the laser–melanosome interaction mechanism by using high-speed imaging. Pigmented p

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Kuroda, Taruho S., Hiroyoshi Ariga, and Mitsunori Fukuda. "The Actin-Binding Domain of Slac2-a/Melanophilin Is Required for Melanosome Distribution in Melanocytes." Molecular and Cellular Biology 23, no. 15 (2003): 5245–55. http://dx.doi.org/10.1128/mcb.23.15.5245-5255.2003.

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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 putat

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Nascimento, Alexandra A. C., Rita G. Amaral, João C. S. Bizario, Roy E. Larson, and Enilza M. Espreafico. "Subcellular Localization of Myosin-V in the B16 Melanoma Cells, a Wild-type Cell Line for the dilute Gene." Molecular Biology of the Cell 8, no. 10 (1997): 1971–88. http://dx.doi.org/10.1091/mbc.8.10.1971.

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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

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Leonhardt, Ralf M., Nathalie Vigneron, Jia Shee Hee, Morven Graham, and Peter Cresswell. "Critical residues in the PMEL/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils." Molecular Biology of the Cell 24, no. 7 (2013): 964–81. http://dx.doi.org/10.1091/mbc.e12-10-0742.

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PMEL (also called Pmel17 or gp100) is a melanocyte/melanoma-specific glycoprotein that plays a critical role in melanosome development by forming a fibrillar amyloid matrix in the organelle for melanin deposition. Although ultimately not a component of mature fibrils, the PMEL N-terminal region (NTR) is essential for their formation. By mutational analysis we establish a high-resolution map of this domain in which sequence elements and functionally critical residues are assigned. We show that the NTR functions in cis to drive the aggregation of the downstream polycystic kidney disease (PKD) do

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Rachinger, Nicole, Nora Mittag, Ines Böhme-Schäfer, Wei Xiang, Silke Kuphal, and Anja K. Bosserhoff. "Alpha-Synuclein and Its Role in Melanocytes." Cells 11, no. 13 (2022): 2087. http://dx.doi.org/10.3390/cells11132087.

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Pigmentation is an important process in skin physiology and skin diseases and presumably also plays a role in Parkinson’s disease (PD). In PD, alpha-Synuclein (aSyn) has been shown to be involved in the pigmentation of neurons. The presynaptic protein is intensively investigated for its pathological role in PD, but its physiological function remains unknown. We hypothesized that aSyn is both involved in melanocytic differentiation and melanosome trafficking processes. We detected a strong expression of aSyn in human epidermal melanocytes (NHEMs) and observed its regulation in melanocytic diffe

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Ando, Hideya, Satoshi Yoshimoto, Moemi Yoshida, et al. "Dermal Fibroblasts Internalize Phosphatidylserine-Exposed Secretory Melanosome Clusters and Apoptotic Melanocytes." International Journal of Molecular Sciences 21, no. 16 (2020): 5789. http://dx.doi.org/10.3390/ijms21165789.

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Pigmentation in the dermis is known to be caused by melanophages, defined as melanosome-laden macrophages. In this study, we show that dermal fibroblasts also have an ability to uptake melanosomes and apoptotic melanocytes. We have previously demonstrated that normal human melanocytes constantly secrete melanosome clusters from various sites of their dendrites. After adding secreted melanosome clusters collected from the culture medium of melanocytes, time-lapse imaging showed that fibroblasts actively attached to the secreted melanosome clusters and incorporated them. Annexin V staining revea

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GOGOI, Bibhuti, Hiredya CHAUHAN, Gaurav HAZARIKA, Amiya BARUAH, Mukunda SAIKIA, and Pallab Jyoti HAZARIKA. "Significance of viscous folding in the migmatites of Chotanagpur Granite Gneiss Complex, eastern India." Earth and Environmental Science Transactions of the Royal Society of Edinburgh 111, no. 2 (2020): 119–34. http://dx.doi.org/10.1017/s1755691020000067.

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ABSTRACTTo understand the physico-chemical processes associated with migmatisation is an interesting petrological problem. New developments in microfluidics and chaotic mixing experiments have helped us to better perceive these processes from the migmatic rocks of the Proterozoic Chotanagpur Granite Gneiss Complex (CGGC), eastern India. The migmatic rocks of CGGC have preserved folded leucocratic veins in amphibolites representing viscous folding. The viscous folding phenomenon occurred due to the interaction between leucosome and melanosome. Based on textural features and mineral chemical dat

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Sitaram, Anand, Rosanna Piccirillo, Ilaria Palmisano, et al. "Localization to Mature Melanosomes by Virtue of Cytoplasmic Dileucine Motifs Is Required for Human OCA2 Function." Molecular Biology of the Cell 20, no. 5 (2009): 1464–77. http://dx.doi.org/10.1091/mbc.e08-07-0710.

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Oculocutaneous albinism type 2 is caused by defects in the gene OCA2, encoding a pigment cell-specific, 12-transmembrane domain protein with homology to ion permeases. The function of the OCA2 protein remains unknown, and its subcellular localization is under debate. Here, we show that endogenous OCA2 in melanocytic cells rapidly exits the endoplasmic reticulum (ER) and thus does not behave as a resident ER protein. Consistently, exogenously expressed OCA2 localizes within melanocytes to melanosomes, and, like other melanosomal proteins, localizes to lysosomes when expressed in nonpigment cell

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Sitaram, Anand, and Michael S. Marks. "Mechanisms of Protein Delivery to Melanosomes in Pigment Cells." Physiology 27, no. 2 (2012): 85–99. http://dx.doi.org/10.1152/physiol.00043.2011.

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Vertebrate pigment cells in the eye and skin are useful models for cell types that use specialized endosomal trafficking pathways to partition cargo proteins to unique lysosome-related organelles such as melanosomes. This review describes current models of protein trafficking required for melanosome biogenesis in mammalian melanocytes.

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Li, Ruoshuang, Liliana D’Alba, Gerben Debruyn, et al. "Mesozoic mammaliaforms illuminate the origins of pelage coloration." Science 387, no. 6739 (2025): 1193–98. https://doi.org/10.1126/science.ads9734.

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Pelage coloration, which serves numerous functions, is crucial to the evolution of behavior, physiology, and habitat preferences of mammals. However, little is known about the coloration of Mesozoic mammaliaforms that coevolved with dinosaurs. In this study, we used a dataset of melanosome (melanin-containing organelle) morphology and quantitatively measured hair colors from 116 extant mammals to reliably reconstruct the coloration of six Mesozoic mammaliaforms, including a previously undescribed euharamiyidan. Unlike the highly diverse melanosomes discovered in feathered dinosaurs, hairs in s

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Harriger, M. Dana, and Steven T. Boyce. "Human melanocytes transfer pigment to epidermal keratinocytes after grafting of a cultured skin substitute to athymic mice." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 400–401. http://dx.doi.org/10.1017/s0424820100147831.

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Melanocytes are pigment-synthesizing cells intercalated among the basal keratinocytes along the dermal-epidermal junction of the skin. Through production of melanin, melanocytes generate skin pigmentation that provides the ultraviolet barrier in the epidermis. Melanosomes are very electron-dense, membrane-bound organelles that package and transfer pigment throughout the epidermis. Melanocytes transfer melanosomes to nearby keratinocytes in the basal layer of the epidermis. The mechanism of pigment transfer may involve either the fusion and breakdown of plasma membranes of both melanocyte and k

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Crawford, Melissa, Nancy Liu, Elahe Mahdipour, Kevin Barr, Bryan Heit, and Lina Dagnino. "Integrin-linked kinase regulates melanosome trafficking and melanin transfer in melanocytes." Molecular Biology of the Cell 31, no. 8 (2020): 768–81. http://dx.doi.org/10.1091/mbc.e19-09-0510.

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Inactivation of the Ilk gene in primary mouse melanocytes results in microtubule defects, impairing normal trafficking of melanosomes toward cell dendrites. Melanosome movements can be restored upon taxol-induced microtubule stabilization. ILK-deficient melanocytes also fail to form normal dendritic extensions through GSK-3–dependent activity. Together, these abnormalities lead to impaired melanin transfer to neighboring epidermal keratinocytes.

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Rossi, Valentina, Maria E. McNamara, Sam M. Webb, Shosuke Ito, and Kazumasa Wakamatsu. "Tissue-specific geometry and chemistry of modern and fossilized melanosomes reveal internal anatomy of extinct vertebrates." Proceedings of the National Academy of Sciences 116, no. 36 (2019): 17880–89. http://dx.doi.org/10.1073/pnas.1820285116.

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Recent discoveries of nonintegumentary melanosomes in extant and fossil amphibians offer potential insights into the physiological functions of melanin not directly related to color production, but the phylogenetic distribution and evolutionary history of these internal melanosomes has not been characterized systematically. Here, we present a holistic method to discriminate among melanized tissues by analyzing the anatomical distribution, morphology, and chemistry of melanosomes in various tissues in a phylogenetically broad sample of extant and fossil vertebrates. Our results show that intern

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Koirala, Mahesh, H. B. Mihiri Shashikala, Jacob Jeffries, et al. "Computational Investigation of the pH Dependence of Stability of Melanosome Proteins: Implication for Melanosome formation and Disease." International Journal of Molecular Sciences 22, no. 15 (2021): 8273. http://dx.doi.org/10.3390/ijms22158273.

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Intravesicular pH plays a crucial role in melanosome maturation and function. Melanosomal pH changes during maturation from very acidic in the early stages to neutral in late stages. Neutral pH is critical for providing optimal conditions for the rate-limiting, pH-sensitive melanin-synthesizing enzyme tyrosinase (TYR). This dramatic change in pH is thought to result from the activity of several proteins that control melanosomal pH. Here, we computationally investigated the pH-dependent stability of several melanosomal membrane proteins and compared them to the pH dependence of the stability of

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Lee, Ki Won, Dang Thi Nguyen, Minju Kim, et al. "Amorphigenin from Amorpha fruticosa L. Root Extract Induces Autophagy-Mediated Melanosome Degradation in mTOR-Independent- and AMPK-Dependent Manner." Current Issues in Molecular Biology 44, no. 7 (2022): 2856–67. http://dx.doi.org/10.3390/cimb44070196.

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In this study, we investigated the depigmentation effect of Amorpha fruticosa L. root extract (RE), an herbal medicine. A. fruticosa RE significantly induced depigmentation in α-MSH-treated B16F10 cells at noncytotoxic concentrations. Further, the RE decreased the protein levels of the melanosomal proteins Tyr and Pmel without decreasing their transcript levels. We found that MG132, a proteasome complex inhibitor, was unable to rescue the protein levels, but PepA/E-64D (a lysosomal enzyme inhibitor), 3-MA (a representative autophagy inhibitor), and ATG5 knockdown effectively rescued the protei

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Bovard, Karen K., and Chhanda Bewtra. "Amelanotic malignant melanoma: recognizing aberrant premelanosomes." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 996–97. http://dx.doi.org/10.1017/s0424820100141354.

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The key to diagnosing cases of melanoma, a tumor of melanocytes, is to recognize cytoplasmic pigment called melanin. In most cases this can be done at the light microscopy level; however, in the rarer amelanotic (non-pigmented) melanomas, melanin is not present in detectable amounts. Thus it is necessary to do an ultxastructural investigation to detect melanosomes, the specific organelles of the melanocyte that synthesize melanin. Other non-melanoma cells can also possess melanin by internalization of melanin granules by phagocytosis or passive transfer (e.g. macrophages, keratinocytes) but th

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Itou, Takashi, Shosuke Ito, and Kazumasa Wakamatsu. "Effects of Aging on Hair Color, Melanosome Morphology, and Melanin Composition in Japanese Females." International Journal of Molecular Sciences 20, no. 15 (2019): 3739. http://dx.doi.org/10.3390/ijms20153739.

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In a previous study, we showed that the size of melanosomes isolated from Japanese female hairs enlarges with age, and this affects the hair color. In this study, we analyzed the age-dependent changes in hair melanin in order to further explore the factors related to hair color changing by aging. A significant positive correlation with age was found in the total melanin amount (TM) and the mol% of 5,6-dihydroxyindole (DHI) units, while no correlation was found in pheomelanin mol%. TM showed significant correlations with hair color parameters and the melanosome volume, suggesting that hair colo

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Rogers, Stephen L., Ryan L. Karcher, Joseph T. Roland, Alexander A. Minin, Walter Steffen, and Vladimir I. Gelfand. "Regulation of Melanosome Movement in the Cell Cycle by Reversible Association with Myosin V." Journal of Cell Biology 146, no. 6 (1999): 1265–76. http://dx.doi.org/10.1083/jcb.146.6.1265.

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Previously, we have shown that melanosomes of Xenopus laevis melanophores are transported along both microtubules and actin filaments in a coordinated manner, and that myosin V is bound to purified melanosomes (Rogers, S., and V.I. Gelfand. 1998. Curr. Biol. 8:161–164). In the present study, we have demonstrated that myosin V is the actin-based motor responsible for melanosome transport. To examine whether myosin V was regulated in a cell cycle-dependent manner, purified melanosomes were treated with interphase- or metaphase-arrested Xenopus egg extracts and assayed for in vitro motility along

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Hume, Alistair N., Lucy M. Collinson, Andrzej Rapak, Anita Q. Gomes, Colin R. Hopkins, and Miguel C. Seabra. "Rab27a Regulates the Peripheral Distribution of Melanosomes in Melanocytes." Journal of Cell Biology 152, no. 4 (2001): 795–808. http://dx.doi.org/10.1083/jcb.152.4.795.

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Rab GTPases are regulators of intracellular membrane traffic. We report a possible function of Rab27a, a protein implicated in several diseases, including Griscelli syndrome, choroideremia, and the Hermansky-Pudlak syndrome mouse model, gunmetal. We studied endogenous Rab27a and overexpressed enhanced GFP-Rab27a fusion protein in several cultured melanocyte and melanoma-derived cell lines. In pigmented cells, we observed that Rab27a decorates melanosomes, whereas in nonpigmented cells Rab27a colocalizes with melanosome-resident proteins. When dominant interfering Rab27a mutants were expressed

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