The melanosome: membrane dynamics in black and white (original) (raw)
Dell'Angelica, E. C., Mullins, C., Caplan, S. & Bonifacino, J. S. Lysosome-related organelles. FASEB J.14, 1265–1278 (2000). ArticleCASPubMed Google Scholar
Seiji, M., Fitzpatrick, T. M., Simpson, R. T. & Birbeck, M. S. C. Chemical composition and terminology of specialized organelles (melanosomes and melanin granules) in mammalian melanocytes. Nature197, 1082–1084 (1963). ArticleCASPubMed Google Scholar
Hearing, V. J. Biochemical control of melanogenesis and melanosomal organization. J. Invest. Dermatol. Symp. Proc.4, 24–28 (1999). ArticleCAS Google Scholar
Schraermeyer, U. & Heimann, K. Current understanding on the role of retinal pigment epithelium and its pigmentation. Pigment Cell Res.12, 219–236 (1999). ArticleCASPubMed Google Scholar
Oetting, W. S. & King, R. A. Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. Human Mutation13, 99–115 (1999). ArticleCASPubMed Google Scholar
Bennett, D. C., Cooper, P. J. & Hart, I. R. A line of non-tumorigenic mouse melanocytes, syngeneic with the B16 melanoma and requiring a tumour promoter for growth. Int. J. Cancer39, 414–418 (1987). ArticleCASPubMed Google Scholar
Kantheti, P. et al. Mutation in AP-3δ in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles. Neuron21, 111–122 (1998).References8, 9and10describe the defect in AP-3 found in mouse and human models of HPS, and are the key references inferring that transporting defects underlie HPS in general. ArticleCASPubMed Google Scholar
Feng, L. et al. The β3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak syndrome and night blindness. Hum. Mol. Genet.8, 323–330 (1999). ArticleCASPubMed Google Scholar
Dell'Angelica, E. C., Shotelersuk, V., Aguilar, R. C., Gahl, W. A. & Bonifacino, J. S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor. Mol. Cell3, 11–21 (1999). ArticleCASPubMed Google Scholar
Huang, L., Kuo, Y. M. & Gitschier, J. The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency. Nature Genet.23, 329–332 (1999). ArticleCASPubMed Google Scholar
Wilson, S. M. et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc. Natl Acad. Sci. USA97, 7933–7938 (2000). ArticleCASPubMedPubMed Central Google Scholar
Ménasché, G. et al. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nature Genet.25, 173–176 (2000).The first demonstration that Griscelli syndrome is heterogeneous, and that the classic syndrome is caused by mutations inRab27a. ArticlePubMed Google Scholar
Detter, J. C. et al. Rab geranylgeranyl transferase α mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis. Proc. Natl Acad. Sci. USA97, 4144–4149 (2000). ArticleCASPubMedPubMed Central Google Scholar
Maul, G. G. Golgi–melanosome relationship in human melanoma in vitro. J. Ultrasctruct. Res.26, 163–176 (1969). ArticleCAS Google Scholar
Kobayashi, T. et al. The Pmel 17/silver locus protein. Characterization and investigation of its melanogenic function. J. Biol. Chem.269, 29198–29205 (1994). CASPubMed Google Scholar
Berson, J. F., Harper, D., Tenza, D., Raposo, G. & Marks, M. S. Pmel17 initiates premelanosomal striation formation within multivesicular bodies. Mol. Biol. Cell (in the press).
Raposo, G., Tenza, D., Murphy, D. M., Berson, J. F. & Marks, M. S. Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells. J. Cell Biol.152, 809–823 (2001).Describes the model for melanosome biogenesis discussed in this review and is the first paper to demonstrate a distinction between melanosomes and lysosomes. ArticleCASPubMedPubMed Central Google Scholar
Futter, C. E., Pearse, A., Hewlett, L. J. & Hopkins, C. R. Multivesicular endosomes containing internalized EGF–EGF receptor complexes mature and then fuse directly with lysosomes. J. Cell Biol.132, 1011–123 (1996). ArticleCASPubMed Google Scholar
Prekeris, R., Yang, B., Oorschot, V., Klumperman, J. & Scheller, R. H. Differential roles of syntaxin 7 and syntaxin 8 in endosomal trafficking. Mol. Biol. Cell10, 3891–3908 (1999). ArticleCASPubMedPubMed Central Google Scholar
Dell'Angelica, E. C., Klumperman, J., Stoorvogel, W. & Bonifacino, J. S. Association of the AP-3 adaptor complex with clathrin. Science280, 431–434 (1998). ArticleCASPubMed Google Scholar
Le Borgne, R., Alconada, A., Bauer, U. & Hoflack, B. The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J. Biol. Chem.273, 29451–29461 (1998). ArticleCASPubMed Google Scholar
Yang, W., Li, C., Ward, D. M., Kaplan, J. & Mansour, S. L. Defective organellar membrane protein trafficking in Ap3b1-deficient cells. J. Cell Sci.113, 4077–4086 (2000). CASPubMed Google Scholar
Heijnen, H. F. et al. Multivesicular bodies are an intermediate stage in the formation of platelet alpha-granules. Blood91, 2313–2325 (1998). CASPubMed Google Scholar
Youssefian, T. & Cramer, E. M. Megakaryocyte dense granule components are sorted in multivesicular bodies. Blood95, 4004–4007 (2000). CASPubMed Google Scholar
Kobayashi, T. et al. The tetraspanin CD63/lamp3 cycles between endocytic and secretory compartments in human endothelial cells. Mol. Biol. Cell11, 1829–1843 (2000). ArticleCASPubMedPubMed Central Google Scholar
Arribas, M. & Cutler, D. F. Weibel–Palade body membrane proteins exhibit differential trafficking after exocytosis in endothelial cells. Traffic1, 783–793 (2000). ArticleCASPubMed Google Scholar
Babst, M., Odorizzi, G., Estepa, E. J. & Emr, S. D. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic1, 248–258 (2000). ArticleCASPubMed Google Scholar
Odorizzi, G., Babst, M. & Emr, S. D. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell95, 847–858 (1998). ArticleCASPubMed Google Scholar
Bishop, N. & Woodman, P. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. J. Biol. Chem.276, 11735–11742 (2001). ArticleCASPubMed Google Scholar
Yoshimori, T. et al. The mouse SKD1, a homologue of yeast Vps4p, is required for normal endosomal trafficking and morphology in mammalian cells. Mol. Biol. Cell11, 747–763 (2000). ArticleCASPubMedPubMed Central Google Scholar
Faigle, W. et al. Deficient peptide loading and MHC class II endosomal sorting in a human genetic immunodeficiency disease: the Chediak-Higashi syndrome. J. Cell Biol.141, 1121–1134 (1998).This paper describes the late endosomal/ lysosomal protein sorting defects observed in Chediak Higashi syndrome, using B lymphocytes as a model. ArticleCASPubMedPubMed Central Google Scholar
Zhao, H. et al. On the analysis of the pathophysiology of Chediak-Higashi syndrome. Defects expressed by cultured melanocytes. Lab Invest.71, 25–34 (1994). CASPubMed Google Scholar
Novikoff, A. B., Albala, A. & Biempica, L. Ultrastructural and cytochemical observations on B-16 and Harding-Passey mouse melanomas. The origin of premelanosomes and compound melanosomes. J. Histochem. Cytochem.16, 299–319 (1968). ArticleCASPubMed Google Scholar
Maul, G. G. & Brumbaugh, J. A. On the possible function of coated vesicles in melanogenesis of the regenerating fowl feather. J. Cell Biol.48, 41–48 (1971). ArticleCASPubMedPubMed Central Google Scholar
Vijayasaradhi, S., Xu, Y. Q., Bouchard, B. & Houghton, A. N. Intracellular sorting and targeting of melanosomal membrane proteins: identification of signals for sorting of the human brown locus protein, gp75. J. Cell Biol.130, 807–820 (1995).The first paper to show that targeting signals for integral membrane transport to melanosomes and to lysosomes are similar. ArticleCASPubMed Google Scholar
Calvo, P. A., Frank, D. W., Bieler, B. M., Berson, J. F. & Marks, M. S. A cytoplasmic sequence in human tyrosinase defines a second class of di-leucine-based sorting signals for late endosomal and lysosomal delivery. J. Biol. Chem.274, 12780–12789 (1999). ArticleCASPubMed Google Scholar
Simmen, T., Schmidt, A., Hunziker, W. & Beermann, F. The tyrosinase tail mediates sorting to the lysosomal compartment in MDCK cells via a di-leucine and a tyrosine-based signal. J. Cell Sci.112, 45–53 (1999). CASPubMed Google Scholar
Blagoveshchenskaya, A. D., Hewitt, E. W. & Cutler, D. F. Di-leucine signals mediate targeting of tyrosinase and synaptotagmin to synaptic-like microvesicles within PC12 cells. Mol. Biol. Cell10, 3979–3990 (1999). ArticleCASPubMedPubMed Central Google Scholar
Kirchhausen, T. Adaptors for clathrin-mediated traffic. Annu. Rev. Cell Dev. Biol.15, 705–732 (1999). ArticleCASPubMed Google Scholar
Höning, S., Sandoval, I. V. & von Figura, K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J.17, 1304–1314 (1998). ArticlePubMedPubMed Central Google Scholar
Liu, T. F., Kandala, G. & Setaluri, V. PDZ-domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase related protein–1). J. Biol. Chem.http://www.jbc.org/cgi/reprint/M103585200v1 (2001).
Anikster, Y. et al. Mutation of a new gene causes a unique form of Hermansky–Pudlak syndrome in a genetic isolate of central Puerto Rico. Nature Genet.28, 376–380 (2001). ArticleCASPubMed Google Scholar
Puri, N., Gardner, J. M. & Brilliant, M. H. Aberrant pH of melanosomes in Pink-Eyed Dilution (p) mutant melanocytes. J. Invest. Dermatol.115, 607–613 (2000). ArticleCASPubMed Google Scholar
Orlow, S. J. & Brilliant, M. H. The pink-eyed dilution locus controls the biogenesis of melanosomes and levels of melanosomal proteins in the eye. Exp. Eye Res.68, 147–154 (1999). ArticleCASPubMed Google Scholar
Manga, P., Boissy, R. E., Pifko-Hirst, S., Zhou, B. K. & Orlow, S. J. Mislocalization of melanosomal proteins in melanocytes from mice with oculocutaneous albinism type 2. Exp. Eye Res.72, 695–710 (2001). ArticleCASPubMed Google Scholar
Fukamachi, S., Shimada, A. & Shima, A. Mutations in the gene encoding B, a novel transporter protein, reduce melanin content in medaka. Nature Genet.28, 381–385 (2001). ArticleCASPubMed Google Scholar
Brilliant, M. H. The mouse p (pink-eyed dilution) and human P genes, oculocutaneous albinism type 2 (OCA2), and melanosomal pH. Pigment Cell Res.14, 86–93 (2001). ArticleCASPubMed Google Scholar
Ungermann, C., Wickner, W. & Xu, Z. Vacuole acidification is required for _trans_-SNARE pairing, LMA1 release, and homotypic fusion. Proc. Natl Acad. Sci. USA96, 11194–11199 (1999). ArticleCASPubMedPubMed Central Google Scholar
Orlow, S. J. Melanosomes are specialized members of the lysosomal lineage of organelles. J. Invest. Dermatol.105, 3–7 (1995). ArticleCASPubMed Google Scholar
Klumperman, J., Kuliawat, R., Griffith, J. M., Geuze, H. J. & Arvan, P. Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J. Cell Biol.141, 359–371 (1998). ArticleCASPubMedPubMed Central Google Scholar
Pryor, P. R., Mullock, B. M., Bright, N. A., Gray, S. R. & Luzio, J. P. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol.149, 1053–1062 (2000). ArticleCASPubMedPubMed Central Google Scholar
Luzio, J. P. et al. Lysosome–endosome fusion and lysosome biogenesis. J. Cell Sci.113, 1515–1524 (2000). CASPubMed Google Scholar
Gardner, J. M. et al. The mouse pale ear (ep) mutation is the homologue of human Hermansky–Pudlak syndrome. Proc. Natl Acad. Sci. USA94, 9238–9243 (1997). ArticleCASPubMedPubMed Central Google Scholar
Horikawa, T. et al. Heterozygous HPS1 mutations in a case of Hermansky–Pudlak syndrome with giant melanosomes. Br. J. Dermatol.143, 635–640 (2000). ArticleCASPubMed Google Scholar
Introne, W., Boissy, R. E. & Gahl, W. A. Clinical, molecular, and cell biological aspects of Chediak-Higashi Syndrome. Mol. Genet. Metabolism68, 283–303 (1999). ArticleCAS Google Scholar
Incerti, B. et al. Oa1 knock-out: new insights on the pathogenesis of ocular albinism type 1. Hum. Mol. Genet.9, 2781–2788 (2000). ArticleCASPubMed Google Scholar
Shen, B., Rosenberg, B. & Orlow, S. J. Intracellular distribution and late endosomal effects of the ocular albinism type 1 gene product: consequences of disease-causing mutations and implications for melanosome biogenesis. Traffic2, 202–211 (2001). ArticleCASPubMed Google Scholar
Stinchcombe, J. C., Page, L. J. & Griffiths, G. M. Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak Higashi Syndrome patients. Traffic1, 435–444 (2000). ArticleCASPubMed Google Scholar
Perou, C. M. et al. The Beige/Chediak-Higashi syndrome gene encodes a widely expressed cytosolic protein. J. Biol. Chem272, 29790–29794 (1997). ArticleCASPubMed Google Scholar
Oh, J., Liu, Z. X., Feng, G. H., Raposo, G. & Spritz, R. A. The Hermansky–Pudlak syndrome (HPS) protein is part of a high molecular weight complex involved in biogenesis of early melanosomes. Hum. Mol. Genet.9, 375–385 (2000). ArticleCASPubMed Google Scholar
Schiaffino, M. V. et al. Ocular albinism: evidence for a defect in an intracellular signal transduction system. Nature Genet.23, 108–112 (1999). ArticleCASPubMed Google Scholar
Langford, G. M. Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol.7, 82–88 (1995). ArticleCASPubMed Google Scholar
Goodson, H. V., Valetti, C. & Kreis, T. E. Motors and membrane traffic. Curr. Opin. Cell Biol.9, 18–28 (1999). Article Google Scholar
Rogers, S. L. & Gelfand, V. I. Membrane trafficking, organelle transport, and the cytoskeleton. Curr. Opin. Cell Biol.12, 57–62 (2000). ArticleCASPubMed Google Scholar
Hirokawa, N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science279, 519–526 (1998). ArticleCASPubMed Google Scholar
Cramer, L. P. Myosin VI: Roles for a minus-end directed actin motor in cells. J. Cell Biol.150, F121–F126 (2000). ArticleCASPubMed Google Scholar
Wu, X., Bowers, B., Rao, K., Wei, Q. & Hammer, J. A., Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J. Cell Biol.143, 1899–1918 (1998).This paper was the first tp propose the current model for melanosome transport in melanocytes. ArticleCASPubMedPubMed Central Google Scholar
Provance, D. W. Jr. Wei, M., Ipe, V. & Mercer, J. A. Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. Proc. Natl Acad. Sci. USA93, 14554–14558 (1996). ArticleCASPubMedPubMed Central Google Scholar
Wei, Q., Wu, X. & Hammer, J. A. The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport. J. Muscle Res. Cell Motil.18, 517–527 (1997). ArticleCASPubMed Google Scholar
Tuma, C. M. & Gelfand, V. I. Molecular mechanisms of pigment transport in melanophores. Pigment Cell Res.12, 283–294 (1999). ArticleCASPubMed Google Scholar
Hara, M. et al. Kinesin participates in melanosomal movement along melanocyte dendrites. J. Invest. Dermatol.114, 438–443 (2000). ArticleCASPubMed Google Scholar
Byers, R. H., Yaar, M., Eller, M. S., Jalbert, N. L. & Gilchrest, B. A. Role of cytoplasmic dynein in melanosome transport in human melanocytes. J. Invest. Dermatol.114, 990–997 (2000). ArticleCASPubMed Google Scholar
Vancoillie, G. et al. Colocalization of dynactin subunits p150Glued and p50 with melanosomes in normal human melanocytes. Pigment Cell Res.13, 449–457 (2000). ArticleCASPubMed Google Scholar
Moore, K. J. et al. The murine dilute suppressor gene dsu suppresses the coat-colour phenotype of three pigment mutations that alter melanocyte morphology, d, ash and ln. Genetics119, 933–941 (1988). CASPubMedPubMed Central Google Scholar
Mercer, J. A., Seperack, P. K., Strobel, M. C., Copeland, N. G. & Jenkins, N. A. Novel myosin heavy chain encoded by murine dilute coat colour locus. Nature349, 709–713 (1991).Describes the first cloning of a pigment dilution gene (myosin Va) causing defects in melanosome transport. ArticleCASPubMed Google Scholar
Walker, M. L. et al. Two-headed binding of a processive myosin to F-actin. Nature405, 804–807 (2000). ArticleCASPubMed Google Scholar
Reck-Peterson, S. L., Provance, D. W. Jr. Mooseker, M. S. & Mercer, J. A. Class V myosins. Biochim. Biophys. Acta1496, 36–51 (2000). ArticleCASPubMed Google Scholar
Seperack, P. K., Mercer, J. A., Strobel, M. C., Copeland, N. G. & Jenkins, N. A. Retroviral sequences located within an intron of the dilute gene alter dilute expression in a tissue-specific manner. EMBO J.14, 2326–2332 (1995). ArticleCASPubMedPubMed Central Google Scholar
Tsakraklides, V. et al. Subcellular localization of GFP-myosin-V in live mouse melanocytes. J. Cell Sci.112, 2863–2865 (1999). Google Scholar
Pastural, E. et al. Griscelli disease maps to chromosome 15q21 and is associated with mutations in the Myosin-Va gene. Nature Genet.16, 289–292 (1997). ArticleCASPubMed Google Scholar
Pastural, E. et al. Two genes are responsible for Griscelli syndrome at the same 15q21 locus. Genomics63, 299–306 (2000). ArticleCASPubMed Google Scholar
Huang, J. -D. et al. Direct interaction of microtubule- and actin-based transport motors. Nature397, 267–270 (1999). ArticleCASPubMed Google Scholar
Hume, A. N. et al. Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J. Cell Biol.152, 795–808 (2001).Together with references89and101, this paper provides mechanistic insights into the role of Rab27a and myosin Va in melanosome transport. ArticleCASPubMedPubMed Central Google Scholar
Wu, X. et al. Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J. Cell Sci.114, 1091–1100 (2001). CASPubMed Google Scholar
Pereira-Leal, J. B. & Seabra, M. C. The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily. J. Mol. Biol.301, 1077–1087 (2000). ArticleCASPubMed Google Scholar
Zerial, M. & McBride, H. Rab proteins as membrane organizers. Nature Rev. Mol. Cell Biol.2, 107–119 (2001). ArticleCAS Google Scholar
Segev, N. Ypt and Rab GTPases: insight into functions through novel interactions. Curr. Opin. Cell Biol.13, 500–511 (2001). ArticleCASPubMed Google Scholar
McBride, H. M. et al. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell98, 377–386 (1999). ArticleCASPubMed Google Scholar
Guo, W., Roth, D., Walch-Solimena, C. & Novick, P. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J.18, 1071–1080 (1999). ArticleCASPubMedPubMed Central Google Scholar
Cao, X., Ballew, N. & Barlowe, C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J.17, 2156–2165 (1998). ArticleCASPubMedPubMed Central Google Scholar
Eitzen, G., Will, E., Gallwitz, D., Haas, A. & Wickner, W. Sequential action of two GTPases to promote vacuole docking and fusion. EMBO J.19, 6713–6720 (2000). ArticleCASPubMedPubMed Central Google Scholar
Allan, B. B., Moyer, B. D. & Balch, W. E. Rab1 recruitment of p115 into a _cis_–SNARE complex: programming budding COPII vesicles for fusion. Science289, 444–448 (2000). ArticleCASPubMed Google Scholar
Carroll, K. S. et al. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science292, 1373–1376 (2001). ArticleCASPubMed Google Scholar
Echard, A. et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science279, 580–585 (1998). ArticleCASPubMed Google Scholar
Nielsen, E., Severin, F., Backer, J. M., Hyman, A. A. & Zerial, M. Rab5 regulates motility of early endosomes on microtubules. Nature Cell Biol.1, 376–382 (1999). ArticleCASPubMed Google Scholar
Stinchcombe, J. C. et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J. Cell Biol.152, 825–834 (2001).Together with reference103, this paper shows the requirement for Rab27a in lysosome-like organelle secretion, using cytotoxic T cells as a model system. ArticleCASPubMedPubMed Central Google Scholar
Haddad, E. K., Wu, X., Hammer, J. A. R. & Henkart, P. A. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J. Cell Biol.152, 835–842 (2001). ArticleCASPubMedPubMed Central Google Scholar
Scott, G. & Zhao, Q. Rab3a and SNARE proteins: potential regulators of melanosome movement. J. Invest. Dermatol.116, 296–304 (2001). ArticleCASPubMed Google Scholar
Araki, K. et al. Small Gtpase rab3A is associated with melanosomes in melanoma cells. Pigment Cell Res.13, 332–336 (2000). ArticleCASPubMed Google Scholar
Jager, D. et al. Serological cloning of a melanocyte rab guanosine 5′-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library. Cancer Res.60, 3584–3591 (2000). CASPubMed Google Scholar
Seabra, M. C. Membrane association and targeting of prenylated Ras-like GTPases. Cell Signal10, 167–172 (1998). ArticleCASPubMed Google Scholar
Walch-Solimena, C., Collins, R. N. & Novick, P. J. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol.137, 1495–1509 (1997). ArticleCASPubMedPubMed Central Google Scholar
Schott, D., Ho, J., Pruyne, D. & Bretscher, A. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol.147, 791–807 (1999). ArticleCASPubMedPubMed Central Google Scholar
Matesic, L. E. et al. Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice. Proc. Natl Acad. Sci. USA98, 10238–10243 (2001). ArticleCASPubMedPubMed Central Google Scholar
Pereira-Leal, J. B. & Seabra, M. C. Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol. (in the press).
Okazaki, K., Uzuka, M., Morikawa, F., Toda, K. & Seiji, M. Transfer mechanism of melanosomes in epidermal cell culture. J. Invest. Dermatol.67, 541–547 (1976). ArticleCASPubMed Google Scholar
Yamamoto, O. & Bhawan, J. Three modes of melanosome transfers in Caucasian facial skin: hypothesis based on an ultrastructural study. Pigment Cell Res.7, 158–169 (1994). ArticleCASPubMed Google Scholar
Kobayashi, T., Imokawa, G., Bennett, D. C. & Hearing, V. J. Tyrosinase stabilization by Tyrp1 (the brown locus protein). J. Biol. Chem.273, 31801–31805 (1998). ArticleCASPubMed Google Scholar
Halaban, R., Cheng, E., Svedine, S., Aron, R. & Hebert, D. N. Proper folding and endoplasmic reticulum to golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J. Biol. Chem.276, 11933–11938 (2001). ArticleCASPubMed Google Scholar
Swank, R. T., Novak, E. K., McGarry, M. P., Rusiniak, M. E. & Feng, L. Mouse models of Hermansky–Pudlak syndrome: a review. Pigment Cell Res.11, 60–80 (1998). ArticleCASPubMed Google Scholar
Huizing, M., Anikster, Y. & Gahl, W. A. Hermansky–Pudlak syndrome and related disorders of organelle formation. Traffic1, 823–835 (2000). ArticleCASPubMed Google Scholar
Liu, X., Ondek, B. & Williams, D. S. Mutant myosin VIIa causes defective melanosome distribution in the RPE of shaker–1 mice. Nature Genet.19, 117–118 (1998). ArticlePubMedCAS Google Scholar