메뉴 건너뛰기




Volumn 289, Issue 26, 2014, Pages 18137-18151

Lys-63-linked ubiquitination by E3 ubiquitin ligase Nedd4-1 facilitates endosomal sequestration of internalized α-Synuclein

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES;

EID: 84903538644     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.529461     Document Type: Article
Times cited : (56)

References (50)
  • 7
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of α-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • Tofaris, G. K., Razzaq, A., Ghetti, B., Lilley, K. S., and Spillantini, M. G. (2003) Ubiquitination of α-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J. Biol. Chem. 278, 44405-44411
    • (2003) J. Biol. Chem. , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 8
    • 0023931333 scopus 로고
    • Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study
    • Kuzuhara, S., Mori, H., Izumiyama, N., Yoshimura, M., and Ihara, Y. (1988) Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study. Acta Neuropathol. 75, 345-353
    • (1988) Acta Neuropathol. , vol.75 , pp. 345-353
    • Kuzuhara, S.1    Mori, H.2    Izumiyama, N.3    Yoshimura, M.4    Ihara, Y.5
  • 10
    • 84892456555 scopus 로고    scopus 로고
    • Enhanced ubiquitin-dependent degradation by Nedd4 protects against α-synuclein accumulation and toxicity in animal models of Parkinson's disease
    • Davies, S. E., Hallett, P. J., Moens, T., Smith, G., Mangano, E., Kim, H. T., Goldberg, A. L., Liu, J. L., Isacson, O., and Tofaris, G. K. (2014) Enhanced ubiquitin-dependent degradation by Nedd4 protects against α-synuclein accumulation and toxicity in animal models of Parkinson's disease. Neurobiol. Dis. 64, 79-87
    • (2014) Neurobiol. Dis. , vol.64 , pp. 79-87
    • Davies, S.E.1    Hallett, P.J.2    Moens, T.3    Smith, G.4    Mangano, E.5    Kim, H.T.6    Goldberg, A.L.7    Liu, J.L.8    Isacson, O.9    Tofaris, G.K.10
  • 11
    • 0029874436 scopus 로고    scopus 로고
    • WWdomains of Nedd4 bind to the proline-rich PY motifs in the epithelial Naα channel deleted in Liddle's syndrome
    • Staub, O., Dho, S., Henry, P., Correa, J., Ishikawa, T., McGlade, J., and Rotin, D. (1996) WWdomains of Nedd4 bind to the proline-rich PY motifs in the epithelial Naα channel deleted in Liddle's syndrome. EMBO J. 15, 2371-2380
    • (1996) EMBO J. , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Rotin, D.7
  • 13
    • 77951228069 scopus 로고    scopus 로고
    • Calcium activates Nedd4 E3 ubiquitin ligases by releasing the C2 domainmediated auto-inhibition
    • Wang, J., Peng, Q., Lin, Q., Childress, C., Carey, D., and Yang, W. (2010) Calcium activates Nedd4 E3 ubiquitin ligases by releasing the C2 domainmediated auto-inhibition. J. Biol. Chem. 285, 12279-12288
    • (2010) J. Biol. Chem. , vol.285 , pp. 12279-12288
    • Wang, J.1    Peng, Q.2    Lin, Q.3    Childress, C.4    Carey, D.5    Yang, W.6
  • 14
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn, R., and Hicke, L. (2001) Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276, 25974-25981
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 15
    • 84878682977 scopus 로고    scopus 로고
    • Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner
    • Hara, S., Arawaka, S., Sato, H., Machiya, Y., Cui, C., Sasaki, A., Koyama, S., and Kato, T. (2013) Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner. Mol. Biol. Cell 24, 1649-1660
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1649-1660
    • Hara, S.1    Arawaka, S.2    Sato, H.3    Machiya, Y.4    Cui, C.5    Sasaki, A.6    Koyama, S.7    Kato, T.8
  • 16
    • 0038051295 scopus 로고    scopus 로고
    • Arapid method to separate endosomes from lysosomal contents using differential centrifugation and hypotonic lysis of lysosomes
    • Schröter, C. J., Braun, M., Englert, J., Beck, H., Schmid, H., and Kalbacher, H. (1999) Arapid method to separate endosomes from lysosomal contents using differential centrifugation and hypotonic lysis of lysosomes. J. Immunol. Methods 227, 161-168
    • (1999) J. Immunol. Methods , vol.227 , pp. 161-168
    • Schröter, C.J.1    Braun, M.2    Englert, J.3    Beck, H.4    Schmid, H.5    Kalbacher, H.6
  • 17
    • 41249090880 scopus 로고    scopus 로고
    • Monoubiquitylation of α-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells
    • Rott, R., Szargel, R., Haskin, J., Shani, V., Shainskaya, A., Manov, I., Liani, E., Avraham, E., and Engelender, S. (2008) Monoubiquitylation of α-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells. J. Biol. Chem. 283, 3316-3328
    • (2008) J. Biol. Chem. , vol.283 , pp. 3316-3328
    • Rott, R.1    Szargel, R.2    Haskin, J.3    Shani, V.4    Shainskaya, A.5    Manov, I.6    Liani, E.7    Avraham, E.8    Engelender, S.9
  • 21
    • 6544291004 scopus 로고    scopus 로고
    • Human ubiquitin-protein ligase Nedd4: Expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes
    • Anan, T., Nagata, Y., Koga, H., Honda, Y., Yabuki, N., Miyamoto, C., Kuwano, A., Matsuda, I., Endo, F., Saya, H., and Nakao, M. (1998) Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. Genes Cells 3, 751-763
    • (1998) Genes Cells , vol.3 , pp. 751-763
    • Anan, T.1    Nagata, Y.2    Koga, H.3    Honda, Y.4    Yabuki, N.5    Miyamoto, C.6    Kuwano, A.7    Matsuda, I.8    Endo, F.9    Saya, H.10    Nakao, M.11
  • 22
    • 34247504273 scopus 로고    scopus 로고
    • Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway
    • Nikko, E., and André, B. (2007) Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway. Traffic 8, 566-581
    • (2007) Traffic , vol.8 , pp. 566-581
    • Nikko, E.1    André, B.2
  • 23
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu, P. J., Zhou, X. Z., Shen, M., and Lu, K. P. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283, 1325-1328
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 24
    • 77956258196 scopus 로고    scopus 로고
    • The lipid-binding domain of wild type and mutant α-synuclein: Compactness and interconversion between the broken and extended helix forms
    • Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., and Eliezer, D. (2010) The lipid-binding domain of wild type and mutant α-synuclein: compactness and interconversion between the broken and extended helix forms. J. Biol. Chem. 285, 28261-28274
    • (2010) J. Biol. Chem. , vol.285 , pp. 28261-28274
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 25
    • 33644954146 scopus 로고    scopus 로고
    • Amino acid sequence motifs and mechanistic features of the membrane translocation of α-synuclein
    • Ahn, K. J., Paik, S. R., Chung, K. C., and Kim, J. (2006) Amino acid sequence motifs and mechanistic features of the membrane translocation of α-synuclein. J. Neurochem. 97, 265-279
    • (2006) J. Neurochem. , vol.97 , pp. 265-279
    • Ahn, K.J.1    Paik, S.R.2    Chung, K.C.3    Kim, J.4
  • 29
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of α-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and Masliah, E. (2013) The many faces of α-synuclein: from structure and toxicity to therapeutic target. Nat. Rev. Neurosci. 14, 38-48
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 30
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren, P. H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., and Kopito, R. R. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219-225
    • (2009) Nat. Cell Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 31
    • 80052690758 scopus 로고    scopus 로고
    • Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking
    • Lin, A., Hou, Q., Jarzylo, L., Amato, S., Gilbert, J., Shang, F., and Man, H. Y. (2011) Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking. J. Neurochem. 119, 27-39
    • (2011) J. Neurochem. , vol.119 , pp. 27-39
    • Lin, A.1    Hou, Q.2    Jarzylo, L.3    Amato, S.4    Gilbert, J.5    Shang, F.6    Man, H.Y.7
  • 32
    • 77955058247 scopus 로고    scopus 로고
    • Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the β2-adrenergic receptor
    • Nabhan, J. F., Pan, H., and Lu, Q. (2010) Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the β2-adrenergic receptor. EMBO Rep. 11, 605-611
    • (2010) EMBO Rep. , vol.11 , pp. 605-611
    • Nabhan, J.F.1    Pan, H.2    Lu, Q.3
  • 33
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • Ingham, R. J., Gish, G., and Pawson, T. (2004) The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 23, 1972-1984
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 36
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin, D., and Kumar, S. (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 10, 398-409
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 37
    • 65649128660 scopus 로고    scopus 로고
    • Lys-63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C., and André, B. (2009) Lys-63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 38
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M., and Haguenauer-Tsapis, R. (1997) Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 40
    • 84866491973 scopus 로고    scopus 로고
    • Endosomal sorting related proteinCHMP2Bis localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy
    • Tanikawa, S., Mori, F., Tanji, K., Kakita, A., Takahashi, H., and Wakabayashi, K. (2012) Endosomal sorting related proteinCHMP2Bis localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy. Neurosci. Lett. 527, 16-21
    • (2012) Neurosci. Lett. , vol.527 , pp. 16-21
    • Tanikawa, S.1    Mori, F.2    Tanji, K.3    Kakita, A.4    Takahashi, H.5    Wakabayashi, K.6
  • 42
    • 0027538111 scopus 로고
    • An early cytoplasmic change before Lewy body maturation: An ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism
    • Hayashida, K., Oyanagi, S., Mizutani, Y., and Yokochi, M. (1993) An early cytoplasmic change before Lewy body maturation: an ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism. Acta Neuropathol. 85, 445-448
    • (1993) Acta Neuropathol. , vol.85 , pp. 445-448
    • Hayashida, K.1    Oyanagi, S.2    Mizutani, Y.3    Yokochi, M.4
  • 43
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams, R. L., and Urbé, S. (2007) The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell Biol. 8, 355-368
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbé, S.2
  • 44
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo
    • Agromayor, M., and Martin-Serrano, J. (2006) Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. J. Biol. Chem. 281, 23083-23091
    • (2006) J. Biol. Chem. , vol.281 , pp. 23083-23091
    • Agromayor, M.1    Martin-Serrano, J.2
  • 45
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid β deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo, A. M., Peterhoff, C. M., Troncoso, J. C., Gomez-Isla, T., Hyman, B. T., and Nixon, R. A. (2000) Endocytic pathway abnormalities precede amyloid β deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol. 157, 277-286
    • (2000) Am. J. Pathol. , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 46
    • 1242316279 scopus 로고    scopus 로고
    • Niemann-Pick type C disease and Alzheimer's disease: The APP-endosome connection fattens up
    • Nixon, R. A. (2004) Niemann-Pick type C disease and Alzheimer's disease: the APP-endosome connection fattens up. Am. J. Pathol. 164, 757-761
    • (2004) Am. J. Pathol. , vol.164 , pp. 757-761
    • Nixon, R.A.1
  • 48
    • 79953846844 scopus 로고    scopus 로고
    • Aggregation of α-synuclein in S. Cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis
    • Soper, J. H., Kehm, V., Burd, C. G., Bankaitis, V. A., and Lee, V. M. (2011) Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis. J. Mol. Neurosci. 43, 391-405
    • (2011) J. Mol. Neurosci. , vol.43 , pp. 391-405
    • Soper, J.H.1    Kehm, V.2    Burd, C.G.3    Bankaitis, V.A.4    Lee, V.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.