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Volumn 10, Issue 10, 2009, Pages 4428-4434

Role of the ubiquitin proteasome system in regulating skin pigmentation

Author keywords

Fatty acid; Melanin; Melanocyte; Pigmentation; Skin; Tyrosinase

Indexed keywords

FATTY ACID; MELANIN; MONOPHENOL MONOOXYGENASE; UBIQUITIN;

EID: 71649114851     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10104428     Document Type: Review
Times cited : (41)

References (39)
  • 1
    • 33947327697 scopus 로고    scopus 로고
    • Approaches to identify inhibitors of melanin biosynthesis via the quality control of tyrosinase
    • Ando, H.; Kondoh, H.; Ichihashi, M.; Hearing, V.J. Approaches to identify inhibitors of melanin biosynthesis via the quality control of tyrosinase. J. Invest. Dermatol. 2007, 127, 751-761.
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 751-761
    • Ando, H.1    Kondoh, H.2    Ichihashi, M.3    Hearing, V.J.4
  • 2
    • 0019291199 scopus 로고
    • Synthesis and degradation of tyrosinase in cultured melanoma cells
    • Saeki, H.; Oikawa, A. Synthesis and degradation of tyrosinase in cultured melanoma cells. J. Cell. Physiol. 1980, 104, 171-175.
    • (1980) J. Cell. Physiol. , vol.104 , pp. 171-175
    • Saeki, H.1    Oikawa, A.2
  • 3
    • 0031041070 scopus 로고    scopus 로고
    • Transforming growth factor-β1 inhibits basal melanogenesis in B16/F10 mouse melanoma cells by increasing the rate of degradation of tyrosinase and tyrosinase-related protein 1
    • Martinez-Esparza, M.; Jiménez-Cervantes, C.; Beermann, F.; Aparicio, P.; Lozano, J.A.; García-Borrón, J.C. Transforming growth factor-β1 inhibits basal melanogenesis in B16/F10 mouse melanoma cells by increasing the rate of degradation of tyrosinase and tyrosinase-related protein 1. J. Biol. Chem. 1997, 272, 3967-3972.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3967-3972
    • Martinez-Esparza, M.1    Jiménez-Cervantes, C.2    Beermann, F.3    Aparicio, P.4    Lozano, J.A.5    García-Borrón, J.C.6
  • 6
    • 0030912157 scopus 로고    scopus 로고
    • Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
    • Halaban, R.; Cheng, E.; Zhang, Y.; Moellmann, G.; Hanlon, D.; Michalak, M.; Setaluri, V.; Hebert, D.N. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Natl. Acad. Sci. USA 1997, 94, 6210-6215.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6210-6215
    • Halaban, R.1    Cheng, E.2    Zhang, Y.3    Moellmann, G.4    Hanlon, D.5    Michalak, M.6    Setaluri, V.7    Hebert, D.N.8
  • 7
    • 0034728770 scopus 로고    scopus 로고
    • Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase
    • Wang, Y.; Androlewicz, M.J. Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase. Biochem. Biophys. Res. Commun. 2000, 271, 22-27.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 22-27
    • Wang, Y.1    Androlewicz, M.J.2
  • 8
    • 4344568526 scopus 로고    scopus 로고
    • Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase
    • Svedine, S.; Wang, T.; Halaban, R.; Hebert, D.N. Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. J. Cell Sci. 2004, 117, 2937-2949.
    • (2004) J. Cell Sci. , vol.117 , pp. 2937-2949
    • Svedine, S.1    Wang, T.2    Halaban, R.3    Hebert, D.N.4
  • 9
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathway
    • DOI 10.1146/annurev.cellbio.14.1.19
    • Bonifacino, J.S.; Weissman, A.M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Ann. Rev. Cell Dev. Biol. 1998, 14, 19-57. (Pubitemid 29001448)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 10
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • Plemper, R.K.; Wolf, D.H. Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci. 1999, 24, 266-270.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 11
  • 12
    • 3342964089 scopus 로고    scopus 로고
    • 25-Hydroxycholesterol acts in the Golgi compartment to induce degradation of tyrosinase
    • Hall, A.M.; Krishnamoorthy, L.; Orlow, S.J. 25-Hydroxycholesterol acts in the Golgi compartment to induce degradation of tyrosinase. Pigment Cell Res. 2004, 17, 396-406.
    • (2004) Pigment Cell Res. , vol.17 , pp. 396-406
    • Hall, A.M.1    Krishnamoorthy, L.2    Orlow, S.J.3
  • 13
    • 15944424673 scopus 로고    scopus 로고
    • Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation
    • Hall, A.M.; Orlow, S.J. Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation. Pigment Cell Res. 2005, 18, 122-129.
    • (2005) Pigment Cell Res. , vol.18 , pp. 122-129
    • Hall, A.M.1    Orlow, S.J.2
  • 15
    • 0032913013 scopus 로고    scopus 로고
    • Molecular basis of albinism: Mutations and polymorphisms of pigmentation genes associated with albinism
    • Oetting, W.S.; King, R.A. Molecular basis of albinism: Mutations and polymorphisms of pigmentation genes associated with albinism. Hum. Mutat. 1999, 13, 99-115.
    • (1999) Hum. Mutat. , vol.13 , pp. 99-115
    • Oetting, W.S.1    King, R.A.2
  • 16
    • 0034806114 scopus 로고    scopus 로고
    • Oculocutaneous albinism types 1 and 3 are ER retention diseases: Mutation of tyrosinase or Tyrp1 can affect the processing of both mutant and wild-type proteins
    • Toyofuku, K.; Wada, I.; Valencia, J.C.; Kushimoto, T.; Ferrans, V.J.; Hearing, V.J. Oculocutaneous albinism types 1 and 3 are ER retention diseases: Mutation of tyrosinase or Tyrp1 can affect the processing of both mutant and wild-type proteins. FASEB J. 2001, 15, 2149-2161.
    • (2001) FASEB J. , vol.15 , pp. 2149-2161
    • Toyofuku, K.1    Wada, I.2    Valencia, J.C.3    Kushimoto, T.4    Ferrans, V.J.5    Hearing, V.J.6
  • 17
    • 0034697167 scopus 로고    scopus 로고
    • A common temperature-sensitive allelic form of human tyrosinase is retained in the endoplasmic reticulum at the nonpermissive temperature
    • Berson, J.F.; Frank, D.W.; Calvo, P.A.; Bieler, B.M.; Marks, M.S. A common temperature-sensitive allelic form of human tyrosinase is retained in the endoplasmic reticulum at the nonpermissive temperature. J. Biol. Chem. 2000, 275, 12281-12289.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12281-12289
    • Berson, J.F.1    Frank, D.W.2    Calvo, P.A.3    Bieler, B.M.4    Marks, M.S.5
  • 18
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C.; Helenius, A. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 1995, 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 19
    • 0035871219 scopus 로고    scopus 로고
    • The molecular basis of oculocutaneous albinism type 1 (OCA1): Sorting failure and degradation of mutant tyrosinase results in a lack of pigmentation
    • Toyofuku, K.; Wada, I.; Spritz, R.A.; Hearing, V.J. The molecular basis of oculocutaneous albinism type 1 (OCA1): Sorting failure and degradation of mutant tyrosinase results in a lack of pigmentation. Biochem. J. 2001, 355, 259-269.
    • (2001) Biochem. J. , vol.355 , pp. 259-269
    • Toyofuku, K.1    Wada, I.2    Spritz, R.A.3    Hearing, V.J.4
  • 20
    • 0034804854 scopus 로고    scopus 로고
    • Tyrosinase degradation via two pathways during reverse translocation to the cytosol
    • Mosse, C.A.; Hsu, W.; Engelhard, V.H. Tyrosinase degradation via two pathways during reverse translocation to the cytosol. Biochem. Biophys. Res. Commun. 2001, 285, 313-319.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 313-319
    • Mosse, C.A.1    Hsu, W.2    Engelhard, V.H.3
  • 21
    • 0030948755 scopus 로고    scopus 로고
    • Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
    • Petrescu, S.M.; Petrescu, A.J.; Titu, H.N.; Dwek, R.A.; Platt, F.M. Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome. J. Biol. Chem. 1997, 272, 15796-15803.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15796-15803
    • Petrescu, S.M.1    Petrescu, A.J.2    Titu, H.N.3    Dwek, R.A.4    Platt, F.M.5
  • 23
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • de Virgilio, M.; Weninger, H.; Ivessa, N.E. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 1998, 273, 9734-9743.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 24
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems
    • DOI 10.1034/j.1600-0854.2002.31102.x
    • Arvan, P.; Zhao, X.; Ramos-Castaneda, J.; Chang, A. Secretory pathway quality control operating in Golgi, plasmalemmal and endosomal systems. Traffic 2002, 3, 771-780. (Pubitemid 35277003)
    • (2002) Traffic , vol.3 , Issue.11 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 25
    • 0023009780 scopus 로고
    • A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution
    • Tanaka, K.; Ii, K.; Ichihara, A.; Waxman, L.; Goldberg, A.L. A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. J. Biol. Chem. 1986, 261, 15197-15203. (Pubitemid 17218097)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.32 , pp. 15197-15203
    • Tanaka, K.1    Ii, K.2    Ichihara, A.3
  • 26
    • 0024600924 scopus 로고
    • The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes
    • McGuire, M.J.; McCullough, M.L.; Croall, D.E.; DeMartino, G.N. The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes. Biochim. Biophys. Acta 1989, 995, 181-186.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 181-186
    • McGuire, M.J.1    McCullough, M.L.2    Croall, D.E.3    Demartino, G.N.4
  • 28
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A.J. Proteasomes: Multicatalytic proteinase complexes. Biochem. J. 1993, 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 30
    • 0021798139 scopus 로고
    • Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate
    • Dahlmann, B.; Rutschmann, M.; Kuehn, L.; Reinauer, H. Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate. Biochem. J. 1985, 228, 171-177. (Pubitemid 15050262)
    • (1985) Biochemical Journal , vol.228 , Issue.1 , pp. 171-177
    • Dahlmann, B.1    Rutschmann, M.2    Kuehn, L.3    Reinauer, H.4
  • 31
    • 0030094434 scopus 로고    scopus 로고
    • Activation of 20S proteasomes from spinach leaves by fatty acids
    • Watanabe, N.; Yamada, S. Activation of 20S proteasomes from spinach leaves by fatty acids. Plant Cell Physiol. 1996, 37, 147-151. (Pubitemid 126609631)
    • (1996) Plant and Cell Physiology , vol.37 , Issue.2 , pp. 147-151
    • Watanabe, N.1    Yamada, S.2
  • 32
    • 0042734890 scopus 로고    scopus 로고
    • Induction of protein catabolism in myotubes by 15(S)- hydroxyeicosatetraenoic acid through increased expression of the ubiquitin-proteasome pathway
    • Whitehouse, A.S.; Khal, J.; Tisdale, M.J. Induction of protein catabolism in myotubes by 15(S)-hydroxyeicosatetraenoic acid through increased expression of the ubiquitin-proteasome pathway. Br. J. Cancer 2003, 89, 737-745.
    • (2003) Br. J. Cancer , vol.89 , pp. 737-745
    • Whitehouse, A.S.1    Khal, J.2    Tisdale, M.J.3
  • 33
    • 46649101669 scopus 로고    scopus 로고
    • Opposite regulation of CD36 ubiquitination by fatty acids and insulin - Effects on fatty acid uptake
    • Smith, J.; Su, X.; El-Maghrabi, R.; Stahl, P.D.; Abumrad, N.A. Opposite regulation of CD36 ubiquitination by fatty acids and insulin - effects on fatty acid uptake. J. Biol. Chem. 2008, 283, 13578-13585.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13578-13585
    • Smith, J.1    Su, X.2    El-Maghrabi, R.3    Stahl, P.D.4    Abumrad, N.A.5
  • 35
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the x-files
    • DOI 10.1126/science.294.5548.1866
    • Chawla, A.; Repa, J.J.; Evans, R.M.; Mangelsdorf, D.J. Nuclear receptors and lipid physiology: Opening the X-files. Science 2001, 294, 1866-1870. (Pubitemid 33101573)
    • (2001) Science , vol.294 , Issue.5548 , pp. 1866-1870
    • Chawta, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 36
    • 4344701247 scopus 로고    scopus 로고
    • The multi-dimensional regulation of gene expression by fatty acids: Polyunsaturated fats as nutrient sensors
    • Clarke, S.D. The multi-dimensional regulation of gene expression by fatty acids: Polyunsaturated fats as nutrient sensors. Curr. Opin. Lipidol. 2004, 15, 13-18.
    • (2004) Curr. Opin. Lipidol. , vol.15 , pp. 13-18
    • Clarke, S.D.1
  • 37
    • 2442506956 scopus 로고    scopus 로고
    • Fatty acids regulate pigmentation via proteasomal degradation of tyrosinase - A new aspect of ubiquitin-proteasome function
    • Ando, H.; Watabe, H.; Valencia, J.C.; Yasumoto, K.; Furumura, M.; Funasaka, Y.; Oka, M.; Ichihashi, M.; Hearing, V.J. Fatty acids regulate pigmentation via proteasomal degradation of tyrosinase - A new aspect of ubiquitin-proteasome function. J. Biol. Chem. 2004, 279, 15427-15433.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15427-15433
    • Ando, H.1    Watabe, H.2    Valencia, J.C.3    Yasumoto, K.4    Furumura, M.5    Funasaka, Y.6    Oka, M.7    Ichihashi, M.8    Hearing, V.J.9
  • 38
    • 0031711547 scopus 로고    scopus 로고
    • Linoleic acid and α-linolenic acid lightens ultraviolet-induced hyperpigmentation of the skin
    • DOI 10.1007/s004030050320
    • Ando, H.; Ryu, A.; Hashimoto, A.; Oka, M.; Ichihashi, M. Linoleic acid and α-linolenic acid lightens ultraviolet-induced hyperpigmentation of the skin. Arch. Dermatol. Res. 1998, 290, 375-381. (Pubitemid 28408561)
    • (1998) Archives of Dermatological Research , vol.290 , Issue.7 , pp. 375-381
    • Ando, H.1    Ryu, A.2    Hashimoto, A.3    Oka, M.4    Ichihashi, M.5


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