Melanoregulin (MREG) modulates lysosome function in pigment epithelial cells
Open accessAbstract
Melanoregulin (MREG), the product of the Mreg(dsu) gene, is a small highly charged protein, hypothesized to play a role in organelle biogenesis due to its effect on pigmentation in dilute, ashen, and leaden mutant mice. Here we provide evidence that MREG is required in lysosome-dependent phagosome degradation. In the Mreg(-/-) mouse, we show that loss of MREG function results in phagosome accumulation due to delayed degradation of engulfed material. Over time, the Mreg(-/-) mouse retinal pigment epithelial cells accumulate the lipofuscin component, A2E. MREG-deficient human and mouse retinal pigment epithelial cells exhibit diminished activity of the lysosomal hydrolase, cathepsin D, due to defective processing. Moreover, MREG localizes to small intracellular vesicles and associates with the endosomal phosphoinositide, phosphatidylinositol 3,5-biphosphate. Collectively, these studies suggest that MREG is required for lysosome maturation and support a role for MREG in intracellular trafficking.
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ARPE-19 and primary RPE cells ingest OSs in less than 1 h.
“ARPE-19 and primary RPE cells have been shown to ingest OSs in less than 1 h (Gibbs et al., 2003; Damek-Poprawa et al., 2009; Olchawa et al., 2013; Wavre-Shapton et al., 2014)”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Damek-Poprawa et al., 2009
RPE from Mreg−/− mice have decreased levels of the mature cathepsin D enzyme.
“RPE from Mreg−/− mice have decreased levels of the mature enzyme (Damek-Poprawa et al., 2009), and increased secretion of pro-cathepsin D into the extracellular medium (Frost et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Damek-Poprawa et al., 2009
Loss of MREG, an LC3B binding partner, contributes to a delay in phagosome maturation and lysosomal exocytosis, as well as basal laminar thickening in older mice.
“Loss of MREG, an LC3B binding partner contributes to a delay in phagosome maturation (Damek-Poprawa et al., 2009) and lysosomal exocytosis, as well as basal laminar thickening in older mice (Frost et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Damek-Poprawa et al., 2009
Phagosome accumulation is observed in the absence of MREG.
“Phagosome accumulation is observed in the absence of MREG (Damek-Poprawa et al., 2009)”
From Microtubule-associated protein 1 light chain 3B, (LC3B) is necessary to maintain lipid-mediated homeostasis in the retinal pigment epithelium (2018) · cites this paper as Damek-Poprawa et al., 2009
Cites
Kornfeld, S. A., & Mellman, I. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.002411 · Cited by 1,593 · see citing works
ARPE-19, A Human Retinal Pigment Epithelial Cell Line with Differentiated Properties
Dunn, K. C., Aotaki-Keen, A. E., Putkey, F. R., & Hjelmeland, L. M. (1996) · Experimental Eye Research · doi:10.1006/exer.1996.0020 · Cited by 1,334 · see citing works
LYSOSOMAL ENZYMES AND THEIR RECEPTORS
FIGURA, K. V., & Hasilík, A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.001123 · Cited by 921 · see citing works
Hasilík, A., & Neufeld, E. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85585-0 · Cited by 803 · see citing works
Rod outer segment disk shedding in rat retina: relationship to cyclic lighting
LaVail, M. M. (1976) · Science · doi:10.1126/science.982063 · Cited by 689 · see citing works
RPE lipofuscin and its role in retinal pathobiology
Sparrow, J. R., & Boulton, M. (2005) · Experimental Eye Research · doi:10.1016/j.exer.2005.01.007 · Cited by 644 · see citing works
Melanosomes — dark organelles enlighten endosomal membrane transport
Raposo, G., & Marks, M. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2258 · Cited by 587 · see citing works
Aging human RPE: morphometric analysis of macular, equatorial, and peripheral cells.
Feeney-Burns, L., Hilderbrand, E. S., & Eldridge, S. (1984) · PubMed · Cited by 561 · see citing works
Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J
Chow, C. Y., Zhang, Y., Dowling, J. J., Jin, N., Adamska, M., Shiga, K., Szigeti, K., Shy, M. E., Li, J., Zhang, X., et al. (2007) · Nature · doi:10.1038/nature05876 · Cited by 516 · see citing works
Visual cells and the concept of renewal.
Young, R. W. (1976) · PubMed · Cited by 482 · see citing works
Parish, C. A., Hashimoto, M., Nakanishi, K., Dillon, J., & Sparrow, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14609 · Cited by 474 · see citing works
Self-citationTrafficking of lysosomal enzymes in normal and disease states.
Kornfeld, S. A. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112262 · Cited by 452 · see citing works
Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues
Hasilik, A., & Neufeld, E. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85586-2 · Cited by 400 · see citing works
Molday, R. S., & MacKenzie, D. J. (1983) · Biochemistry · doi:10.1021/bi00272a020 · Cited by 391 · see citing works
Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis
Liaudet‐Coopman, E., Beaujouin, M., Derocq, D., Garcia, M., Glondu-Lassis, M., Laurent‐Matha, V., Prébois, C., Rochefort, H., & Vignon, F. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.06.007 · Cited by 353 · see citing works
Pmel17 initiates premelanosome morphogenesis within multivesicular bodies
Berson, J. F., Harper, D. C., Tenza, D., Raposo, G., & Marks, M. S. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3451 · Cited by 326 · see citing works
Loss of synchronized retinal phagocytosis and age-related blindness in mice lacking αvβ5 integrin
Nandrot, E. F., Kim, Y., Brodie, S. E., Huang, X., Sheppard, D., & Finnemann, S. C. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20041447 · Cited by 319 · see citing works
Syntaxin 13 Mediates Cycling of Plasma Membrane Proteins via Tubulovesicular Recycling Endosomes
Prekeris, R., Klumperman, J., Chen, Y. A., & Scheller, R. H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.957 · Cited by 286 · see citing works
Finnemann, S. C., Leung, L. W., & Rodriguez-Boulan, E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052025899 · Cited by 283 · see citing works
Inhibition of lysosomal degradative functions in RPE cells by a retinoid component of lipofuscin.
Holz, F. G., Schütt, F., Kopitz, J., Eldred, G. E., Kruse, F. E., Völcker, H. E., & Cantz, M. (1999) · PubMed · Cited by 280 · see citing works
PARTICIPATION OF THE RETINAL PIGMENT EPITHELIUM IN THE ROD OUTER SEGMENT RENEWAL PROCESS
Young, R. W., & Bok, D. (1969) · Journal of Cell Biology · doi:10.1083/jcb.42.2.392 · Cited by 271 · see citing works
TAM receptor function in the retinal pigment epithelium
Prasad, D., Rothlin, C. V., Burrola, P., Burstyn-Cohen, T., Lu, Q., Garcia de Frutos, P., & Lemke, G. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.06.011 · Cited by 270 · see citing works
Matesic, L. E., Yip, R., Reuss, A. E., Swing, D. A., O’Sullivan, T. N., Fletcher, C., Copeland, N. G., & Jenkins, N. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181336698 · Cited by 258 · see citing works
Liu, J., Itagaki, Y., Ben-Shabat, S., Nakanishi, K., & Sparrow, J. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910191199 · Cited by 255 · see citing works
Gibbs, D., Kitamoto, J., & Williams, D. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1130432100 · Cited by 250 · see citing works
The Quest for the Mechanism of Melanin Transfer
Bossche, K. V. D., Naeyaert, J., & Lambert, J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00425.x · Cited by 246 · see citing works
Phosphatidylinositol 3,5-bisphosphate: metabolism and cellular functions
Michell, R. H., Heath, V. L., Lemmon, M. A., & Dove, S. K. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.013 · Cited by 233 · see citing works
Bergmann, M., Schütt, F., Holz, F. G., & Kopitz, J. (2004) · The FASEB Journal · doi:10.1096/fj.03-0289fje · Cited by 226 · see citing works
Lysosome-related organelles: driving post-Golgi compartments into specialisation
Raposo, G., Marks, M. S., & Cutler, D. F. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.05.001 · Cited by 215 · see citing works
Self-citationCuervo, A. M., & Dice, J. F. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00075-9 · Cited by 215 · see citing works
Biosynthetic Studies of A2E, a Major Fluorophore of Retinal Pigment Epithelial Lipofuscin
Ben-Shabat, S., Parish, C. A., Vollmer, H. R., Itagaki, Y., Fishkin, N., Nakanishi, K., & Sparrow, J. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108981200 · Cited by 214 · see citing works
Histopathology and immunocytochemistry of the neurosensory retina in fundus flavimaculatus.
Birnbach, C., Järveläínen, M., Possin, D., & Milam, A. (1994) · Ophthalmology (Rochester, Minn.) · doi:10.1016/s0161-6420(13)31725-4 · Cited by 212 · see citing works
Circadian nature of rod outer segment disc shedding in the rat.
LaVail, M. M. (1980) · PubMed · Cited by 199 · see citing works
The retinal pigment epithelium : function and disease
Marmor, M. F., & Wolfensberger, T. J. (1998) · Cited by 185 · see citing works
A Histopathologic Study of Best's Macular Dystrophy
Frangieh, G. T., Green, W. R., & Fine, S. (1982) · Archives of Ophthalmology · doi:10.1001/archopht.1982.01030040093017 · Cited by 177 · see citing works
p16Ink4a in Melanocyte Senescence and Differentiation
Sviderskaya, E. V. (2002) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/94.6.446 · Cited by 177 · see citing works
deDuve, C. (1996) · PubMed · Cited by 174 · see citing works
Rakoczy, P. E., Zhang, D., Robertson, T., Barnett, N. L., Papadimitriou, J., Constable, I. J., & Lai, C.-M. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64427-6 · Cited by 173 · see citing works
Azarian, S. M., & Travis, G. H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00517-6 · Cited by 170 · see citing works
The Retinal Pigment Epithelium: Function and Disease
Lyle, W. M. (1999) · Optometry and Vision Science · doi:10.1002/j.1538-9235.1999.tb05362.x · Cited by 167 · see citing works
Yasuda, Y., Kageyama, T., AKAMINE, A., Shibata, M., Kominami, E., Uchiyama, Y., & Yamamoto, K. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022396 · Cited by 163 · see citing works
The building BLOC(k)s of lysosomes and related organelles
Dell’Angelica, E. C. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.05.001 · Cited by 162 · see citing works
Regulated Secretion from Hemopoietic Cells
Stinchcombe, J. C., & Griffiths, G. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.1.1 · Cited by 161 · see citing works
Endosomal Phosphoinositides and Human Diseases
Nicot, A.-S., & Laporte, J. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00754.x · Cited by 153 · see citing works
Immortalization of polarized rat retinal pigment epithelium
Nabi, I. R., Mathews, A. P., Cohen-Gould, L., Gundersen, D., & Rodriguez-Boulan, E. (1993) · Journal of Cell Science · doi:10.1242/jcs.104.1.37 · Cited by 153 · see citing works
Phagocytosis of outer segments by retinal pigment epithelium: phagosome-lysosome interaction
Bosch, E., Horwitz, J., & Bok, D. (1993) · Journal of Histochemistry & Cytochemistry · doi:10.1177/41.2.8419462 · Cited by 147 · see citing works
Kim, S. R., Fishkin, N. E., Kong, J., Nakanishi, K., Allikmets, R. L., & Sparrow, J. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403499101 · Cited by 146 · see citing works
Fishkin, N. E., Sparrow, J. R., Allikmets, R., & Nakanishi, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501266102 · Cited by 146 · see citing works
Self-citationKim, S. R., Jang, Y. P., Jockusch, S., Fishkin, N. E., Turro, N. J., & Sparrow, J. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708714104 · Cited by 145 · see citing works
Feeney-Burns, L., & Ge, E. (1983) · PubMed · Cited by 143 · see citing works
PI3P signaling regulates receptor sorting but not transport in the endosomal pathway
Petiot, A., Fauré, J., Stenmark, H., & Gruenberg, J. E. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303018 · Cited by 142 · see citing works
RP1 Is Required for the Correct Stacking of Outer Segment Discs
Liu, Q., Lyubarsky, A., Skalet, J. H., Pugh, E. N., & Pierce, E. A. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0410 · Cited by 129 · see citing works
Danciger, M., Matthes, M. T., Yasamura, D., Akhmedov, N. B., Rickabaugh, T. M., Gentleman, S., Redmond, T. M., Vail, M. M. L., & Farber, D. B. (2000) · Mammalian Genome · doi:10.1007/s003350010081 · Cited by 127 · see citing works
Usher syndromes due to MYO7A, PCDH15, USH2A or GPR98 mutations share retinal disease mechanism
Jacobson, S. G., Cideciyan, A. V., Alemán, T. S., Sumaroka, A., Román, A. J., Gardner, L. M., Prosser, H. M., Mishra, M., Bech‐Hansen, N. T., Herrera, W., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn140 · Cited by 118 · see citing works
Structural requirements of procathepsin D activation and maturation.
Richo, G. R., & Conner, G. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36696-6 · Cited by 97 · see citing works
LYSOSOMAL DYSFUNCTIONS ASSOCIATED WITH MUTATIONS AT MOUSE PIGMENT GENES
Novak, E. K., & Swank, R. T. (1979) · Genetics · doi:10.1093/genetics/92.1.189 · Cited by 95 · see citing works
Lemansky, P., Gieselmann, V., Hasilík, A., & FIGURA, K. V. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90939-7 · Cited by 84 · see citing works
Mouse coat color mutations: From fancy mice to functional genomics
Steingrı́msson, E., Copeland, N. G., & Jenkins, N. A. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20840 · Cited by 77 · see citing works
Boulton, M., Moriarty, P., Jarvis-Evans, J., & Marcyniuk, B. (1994) · British Journal of Ophthalmology · doi:10.1136/bjo.78.2.125 · Cited by 74 · see citing works
Moore, K. J., Swing, D. A., Rinchik, E. M., Mucenski, M. L., Buchberg, A. M., Copeland, N. G., & Jenkins, N. A. (1988) · Genetics · doi:10.1093/genetics/119.4.933 · Cited by 65 · see citing works
Modulation of cathepsin D activity in retinal pigment epithelial cells
RAKOCZY, P. E., LAI, C. M., BAINES, M., GRANDI, S. D., FITTON, J. H., & CONSTABLE, I. J. (1997) · Biochemical Journal · doi:10.1042/bj3240935 · Cited by 64 · see citing works
Hoppe, G., Marmorstein, A. D., Pennock, E. A., & Hoff, H. F. (2001) · PubMed · Cited by 61 · see citing works
Regan, C. M., de Grip, W. J., Daemen, F. J. M., & Bonting, S. L. (1980) · Experimental Eye Research · doi:10.1016/0014-4835(80)90112-8 · Cited by 60 · see citing works
Dilute suppressor, a new suppressor gene in the house mouse
Sweet, H. O. (1983) · Journal of Heredity · doi:10.1093/oxfordjournals.jhered.a109794 · Cited by 57 · see citing works
Bergmann, M., Schütt, F., Holz, F. G., & Kopitz, J. (2001) · Experimental Eye Research · doi:10.1006/exer.2000.0949 · Cited by 53 · see citing works
Sparrow, J. R., Kim, S. R., Cuervo, A. M., & Bandhyopadhyayand, U. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-74904-4_46 · Cited by 52 · see citing works
Enzymatic deglycosylation of bovine rhodopsin
Plantner, J. J., Le, M.-L., & Kean, E. L. (1991) · Experimental Eye Research · doi:10.1016/0014-4835(91)90083-q · Cited by 51 · see citing works
Chondrocytes Utilize a Cholesterol-Dependent Lipid Translocator To Externalize Phosphatidylserine
Damek-Poprawa, M., Golub, E. E., Otis, L. L., Harrison, G., Phillips, C., & Boesze‐Battaglia, K. (2006) · Biochemistry · doi:10.1021/bi0515927 · Cited by 49 · see citing works
Rakoczy, P. E., Mann, K., Cavaney, D. M., Robertson, T. A., Papadimitreou, J., & Constable, I. J. (1994) · PubMed · Cited by 48 · see citing works
dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice
O’Sullivan, T. N., Wu, X., Rachel, R. A., Huang, J.-D., Swing, D. A., Matesic, L. E., Hammer, J. A., Copeland, N. G., & Jenkins, N. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407339101 · Cited by 46 · see citing works
Hoppe, G., O'NEIL, J. A., Hoff, H. F., & Sears, J. E. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.01.004 · Cited by 45 · see citing works
Proteolytic processing of cathepsin D in prelysosomal organelles.
Delbrück, R., Desel, C., FIGURA, K. V., & Hille‐Rehfeld, A. (1994) · PubMed · Cited by 43 · see citing works
Hoppe, G., O'Neil, J., Hoff, H., & Sears, J. E. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-004-4080-5 · Cited by 42 · see citing works
Isolation and Culture of Primary Mouse Retinal Pigmented Epithelial Cells
Gibbs, D., & Williams, D. S. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0067-4_44 · Cited by 41 · see citing works
Autophagic Defects in Aging: Looking for an “Emergency Exit"?
Massey, A. C., Kiffin, R., & Cuervo, A. M. (2006) · Cell Cycle · doi:10.4161/cc.5.12.2865 · Cited by 41 · see citing works
Accumulation of inactive cathepsin D in old rats
Wiederanders, B., & Oelke, B. (1984) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(84)90112-x · Cited by 40 · see citing works
HYPERLIPOFUSCINOSIS AND SUBRETINAL FIBROSIS IN STARGARDTʼS DISEASE
Laey, J. J. D., & Verougstraete, C. (1995) · Retina · doi:10.1097/00006982-199515050-00005 · Cited by 36 · see citing works
Moore, K. J., Seperack, P. K., Strobel, M. C., Swing, D. A., Copeland, N. G., & Jenkins, N. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8131 · Cited by 35 · see citing works
Boesze‐Battaglia, K., Song, H., Sokolov, M., Lillo, C., Walker, L. M., Gretzula, C., Gallagher, B., Rachel, R. A., Jenkins, N. A., Copeland, N. G., et al. (2007) · Biochemistry · doi:10.1021/bi061466i · Cited by 35 · see citing works
Degradation of rod outer segment proteins by cathepsin D
HAYASAKA, S., HARA, S., & MIZUNO, K. (1975) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131034 · Cited by 34 · see citing works
Phosphoinositides' link to neurodegeneration
Volpicelli‐Daley, L. A., & Camilli, P. V. D. (2007) · Nature Medicine · doi:10.1038/nm0707-784 · Cited by 32 · see citing works
Interaction of the murine dilute suppressor gene (dsu) with fourteen coat color mutations.
Moore, K. J., Swing, D. A., Copeland, N. G., & Jenkins, N. A. (1990) · Genetics · doi:10.1093/genetics/125.2.421 · Cited by 30 · see citing works
Age-related changes of glycosidases in human retinal pigment epithelium
Cingle, K. A., Kalski, R. S., Bruner, W. E., O'brien, C. M., Erhard, P., & Wyszynski, R. E. (1996) · Current Eye Research · doi:10.3109/02713689608995834 · Cited by 29 · see citing works
Verdugo, M. E., & Ray, J. (1997) · Experimental Eye Research · doi:10.1006/exer.1997.0325 · Cited by 27 · see citing works
Vectorial accumulation of cathepsin D in retinal pigmented epithelium: effects of age.
Wilcox, D. K. (1988) · PubMed · Cited by 20 · see citing works
Siakotos, A. N., Armstrong, D., Koppang, N., & Connole, E. (1978) · PubMed · Cited by 16 · see citing works
The murine dilute suppressor gene encodes a cell autonomous suppressor.
Moore, K. J., Swing, D. A., Copeland, N. G., & Jenkins, N. A. (1994) · Genetics · doi:10.1093/genetics/138.2.491 · Cited by 16 · see citing works
Analysis of the Rate of Disk Membrane Digestion by Cultured RPE Cells
Diemer, T., Gibbs, D., & Williams, D. S. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-74904-4_37 · Cited by 11 · see citing works
Marks, M. S. (2007) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2007.00421.x · Cited by 11 · see citing works
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Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422 · see citing works
Ferrington, D. A., Sinha, D., & Kaarniranta, K. (2016) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2015.09.002 · Cited by 241 · see citing works
Understanding photoreceptor outer segment phagocytosis: use and utility of RPE cells in culture
Mazzoni, F., Safa, H., & Finnemann, S. C. (2014) · Experimental Eye Research · doi:10.1016/j.exer.2014.01.010 · Cited by 221 · see citing works
Autophagy in the eye: implications for ocular cell health.
Frost, L. S., Mitchell, C. H., & Boesze-Battaglia, K. (2014) · Experimental Eye Research · doi:10.1016/j.exer.2014.04.010 · Cited by 134 · see citing works
Phagocytosis-dependent ketogenesis in retinal pigment epithelium
Reyes-Reveles, J., Dhingra, A., Alexander, D., Bragin, A., Philp, N. J., & Boesze-Battaglia, K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.770784 · Cited by 116 · see citing works
Melanosomes on the move: a model to understand organelle dynamics
Hume, A. N., & Seabra, M. C. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391191 · Cited by 92 · see citing works
Modifier genes and the plasticity of genetic networks in mice
Hamilton, B. A., & Yu, B. D. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002644 · Cited by 78 · see citing works
Role of Rab family GTPases and their effectors in melanosomal logistics
Ohbayashi, N., & Fukuda, M. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs009 · Cited by 73 · see citing works
Frost, L. S., Lopes, V. S., Bragin, A., Reyes-Reveles, J., Brancato, J., Cohen, A., Mitchell, C. H., Williams, D. S., & Boesze-Battaglia, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-8920-5 · Cited by 63 · see citing works
Self-citationOhbayashi, N., Maruta, Y., Ishida, M., & Fukuda, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.094185 · Cited by 61 · see citing works
Domingo-Gonzalez, R., Zanini, F., Che, X., Liu, M., Jones, R. C., Swift, M. A., Quake, S. R., Cornfield, D. N., & Alvira, C. M. (2020) · eLife · doi:10.7554/elife.56890 · Cited by 56 · see citing works
Sethna, S., Chamakkala, T., Gu, X., Thompson, T. C., Cao, G., Elliott, M. H., & Finnemann, S. C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.687004 · Cited by 53 · see citing works
Dhingra, A., Bell, B. A., Peachey, N. S., Daniele, L. L., Reyes-Reveles, J., Sharp, R. C., Jun, B., Bazan, N. G., Sparrow, J. R., Kim, H. J., et al. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00351 · Cited by 41 · see citing works
Butler, J. M., Supharattanasitthi, W., Yang, Y. C., & Paraoan, L. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16569 · Cited by 42 · see citing works
Multiple A2E treatments lead to melanization of rod outer segment-challenged ARPE-19 cells.
Poliakov, E., Strunnikova, N. V., Jiang, J., Martinez, B., Parikh, T. P., Lakkaraju, A., Thomas, C. J., Brooks, B. P., & Redmond, T. M. (2014) · Europe PMC (PubMed Central) · Cited by 27 · see citing works
Dissanayake, C.-Y., Moon, H.-H., Yang, K.-M., Lee, Y., & Han, C. (2018) · Korean Journal of Veterinary Research · doi:10.14405/kjvr.2018.58.2.65 · Cited by 25 · see citing works
Khalil, S., Enbody, E. D., Frankl‐Vilches, C., Welklin, J. F., Koch, R. E., Toomey, M. B., Sin, S. Y. W., Edwards, S. V., Gahr, M. L., Schwabl, H. G., et al. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad056 · Cited by 23 · see citing works
MREG suppresses thyroid cancer cell invasion and proliferation by inhibiting Akt-mTOR signaling
Meng, X., Dong, Y., Xiao, Y., Wang, D., Wang, S., Chen, S., & Pang, S. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.07.044 · Cited by 22 · see citing works
The Late Endosomal Pathway Regulates the Ciliary Targeting of Tetraspanin Protein Peripherin 2
Otsu, W., Hsu, Y., Chuang, J.-Z., & Sung, C.-H. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2811-18.2019 · Cited by 21 · see citing works
Lipid nanoparticles as a tool to dissect dendritic cell maturation pathways
Rennen, S., Bosteels, V., Nolf, C. D., Maréchal, S., Vetters, J., Lil, K. V., Webb, G. R., Swinnen, J., Velde, E. V. D., Fayazpour, F., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116150 · Cited by 19 · see citing works
Huang, R., Zhe, Z., Wang, Q., Zhao, X., Deng, Y., Jiao, Y., & Du, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141390 · Cited by 19 · see citing works
A novel melano-lysosome in the retinal epithelium of rhesus monkeys
Gouras, P., Brown, K. R., Ivert, L., & Neuringer, M. D. (2011) · Experimental Eye Research · doi:10.1016/j.exer.2011.10.011 · Cited by 19 · see citing works
Melanoregulin is stably targeted to the melanosome membrane by palmitoylation
Wu, X., Martina, J. A., & Hammer, J. A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.08.064 · Cited by 17 · see citing works
Li, A., Wu, N., & Sun, J. (2022) · Oncology Letters · doi:10.3892/ol.2022.13202 · Cited by 17 · see citing works
Grubaugh, C. R., Dhingra, A., Prakash, B., Montenegro, D., Sparrow, J. R., Daniele, L. L., Curcio, C. A., Bell, B. A., Hussain, M. M., & Boesze‐Battaglia, K. (2024) · The FASEB Journal · doi:10.1096/fj.202302491r · Cited by 16 · see citing works
Convergent genomic signatures of local adaptation across a continental-scale environmental gradient
Moreira, L. R., & Smith, B. T. (2023) · Science Advances · doi:10.1126/sciadv.add0560 · Cited by 14 · see citing works
Pinelli, R., Biagioni, F., Limanaqi, F., Bertelli, M., Scaffidi, E., Polzella, M., Busceti, C. L., & Fornai, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155563 · Cited by 14 · see citing works
Cui, X., Kim, H. J., Cheng, C.-H., Jenny, L. A., de Carvalho, J. R. L., Chang, Y.-J., Kong, Y., Hsu, C., Huang, I.-W., Ragi, S. D., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac032 · Cited by 13 · see citing works
Animal Models, in “The Quest to Decipher RPE Phagocytosis”
Nandrot, E. F. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3209-8_10 · Cited by 13 · see citing works
Autophagy in aging-related oral diseases
Peña‐Oyarzún, D., Martin, C. S., Hernández‐Cáceres, M. P., Lavandero, S., Morselli, E., Budini, M., Burgos, P. V., & Criollo, A. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.903836 · Cited by 12 · see citing works
Melanoregulin, Product of the dsu Locus, Links the BLOC-Pathway and Oa1 in Organelle Biogenesis
Rachel, R. A., Nagashima, K., O’Sullivan, T. N., Frost, L. S., Stefano, F. P., Marigo, V., & Boesze‐Battaglia, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042446 · Cited by 12 · see citing works
Microtubule Motor Transport of Organelles in a Specialized Epithelium: The RPE
Hazim, R. A., & Williams, D. S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.852468 · Cited by 10 · see citing works
Campbell, L. J., West, M. C., & Jensen, A. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-32336-y · Cited by 11 · see citing works
Rout, A. K., Wu, X., Starich, M. R., Strub, M., Hammer, J. A., & Tjandra, N. (2018) · Structure · doi:10.1016/j.str.2018.07.009 · Cited by 11 · see citing works
Loss of melanoregulin (MREG) enhances cathepsin-D secretion by the retinal pigment epithelium
FROST, L. S., LOPES, V. S., STEFANO, F. P., BRAGIN, A., WILLIAMS, D. S., MITCHELL, C. H., & BOESZE-BATTAGLIA, K. (2013) · Visual Neuroscience · doi:10.1017/s0952523813000096 · Cited by 9 · see citing works
Milenkovic, A., Schmied, D., Tanimoto, N., Seeliger, M. W., Sparrow, J. R., & Weber, B. H. F. (2019) · Biology Open · doi:10.1242/bio.041335 · Cited by 9 · see citing works
Rahman, M. A., Shaikh, M. H., Gupta, R. D., Siddika, N., Shaikh, M. S., Zafar, M. S., Kim, B., & Apu, E. H. (2024) · Biomedicines · doi:10.3390/biomedicines12112645 · Cited by 8 · see citing works
Krivoruchko, A. Y., Likhovid, A. A., Александровна, К. А., Saprikina, T. Y., Safaryan, E. Y., & Yatsyk, O. A. (2023) · Genes · doi:10.3390/genes14061288 · Cited by 8 · see citing works
Mouse‐specific up‐regulation of Ccnb1 expression by miR‐199a‐5p in keratinocyte
Kim, B., Kim, I. J., Lee, A., Yoo, H., & Yoon, S. K. (2016) · FEBS Open Bio · doi:10.1002/2211-5463.12133 · Cited by 7 · see citing works
Müller, C., & Finnemann, S. C. (2020) · Springer eBooks · doi:10.1007/978-3-030-28384-1_3 · Cited by 6 · see citing works
Genome-wide association study for reproduction traits in Colombian Creole Blanco Orejinegro cattle
Ríos, A. C. H., Nasner, S. L. C., Londoño‐Gil, M., Herrera, L. G. G., Herrera, A. L., & Flórez, J. C. R. (2023) · Tropical Animal Health and Production · doi:10.1007/s11250-023-03847-2 · Cited by 5 · see citing works
Autophagy in Ocular Pathophysiology
Mitter, S. K., & Boulton, M. E. (2016) · InTech eBooks · doi:10.5772/64667 · Cited by 1 · see citing works
Dietary Antioxidants, αvβ5 Integrin, and Ocular Protection
Sethna, S., & Finnemann, S. C. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-401717-7.00058-7
Domingo-Gonzalez, R., Zanini, F., Che, X., Liu, M., Jones, R. C., Swift, M. A., Quake, S. R., Cornfield, D. N., & Alvira, C. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.10.942359
Fukuda, M., & Ohbayashi, N. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733940866.793574988
Müller, C., & Finnemann, S. C. (2024) · Springer eBooks · doi:10.1007/978-3-031-35055-9_3
Lipid nanoparticles as a tool to dissect dendritic cell maturation pathwaysPreprint
Janssens, S., Rennen, S., Bosteels, V., Nolf, C. D., Lil, K. V., Maréchal, S., Vetters, J., Velde, E. V. D., Fayazpour, F., Roelandt, R., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-5461735/v1
Melanoregulin Deficiency Affects Bone Maintenance and Lean Body MassPreprint
Musskopf, M. L., Gonçalves, V. D. P., Tuin, S. A., Wong, S., Boesze‐Battaglia, K., & Miguez, P. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.14.691656
Chen, Z., Huang, C., Zhu, H., Xiao, S., Zhou, D., Su, H., Xiang, Y., Chen, Z., Wen, S., Zhao, H., et al. (2026) · Journal of Genetics · doi:10.1007/s12041-025-01519-8
Usin, S. G., Olajire, G. A., Olumese, J. O., Idenyi, E. O., Oluwafemi, O., Oluwasola, T., Salami, A. A., Omotuyi, O. I., Ogun, G., & Gbadegesin, M. A. (2026) · BMC Cancer · doi:10.1186/s12885-026-15972-w
- Authors
- Damek-Poprawa, M., Diemer, T., Lopes, V. S., Lillo, C., Harper, D. C., Marks, M. S., Wu, Y., Sparrow, J. R., Rachel, R. A., Williams, D. S., & Boesze-Battaglia, K.
- Affiliations
- University of Pennsylvania (US)
- University of California, Los Angeles (US)
- University of California San Diego (US)
- Columbia University (US)
- National Institutes of Health (US)
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-04
- Volume
- 284
- Issue
- 16
- Pages
- 10877-10889
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2667774
- OpenAlex
- W2093780646
- Cited by
- 50
- References
- 89
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 1 · 2020: 6 · 2019: 2 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 6 · 2013: 1 · 2012: 5
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ScholarlyCommons (University of Pennsylvania) (submittedVersion)
- Funders
- National Institutes of Health (5p30ey012598-05)
- National Eye Institute (R01EY012951, EY 12951, R01EY010420, R21EY018705, EY-15625, P30-EY12598, EY-00331, R01EY007042, EY07042, R29EY010420, R01EY015625, P30EY001583, EY-10420)
- National Center for Research Resources (S10RR026365)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
- Keywords
- lysosome maturation, retinal pigment epithelial cells, lipofuscin, A2E, cathepsin D, phosphatidylinositol 3,5-bisphosphate, endosomal trafficking, organelle biogenesis
- MeSH terms
- Animals, Carrier Proteins, Cathepsin D, Cell Line, Epithelial Cells, Humans, Lipofuscin, Lysosomes, Mice, Inbred C57BL, Phagocytosis, Phosphatidylethanolamines, Pigment Epithelium of Eye, Pyridinium Compounds, Retinaldehyde, Retinoids, Phosphatidylinositol Phosphates, Mice, Knockout, Adaptor Proteins, Vesicular Transport, RNA, Small Interfering, Intracellular Signaling Peptides and Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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