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Volumn 12, Issue 3, 2011, Pages 330-348

Alzheimer's Disease-Associated Ubiquilin-1 Regulates Presenilin-1 Accumulation and Aggresome Formation

Author keywords

amyloid precursor protein; High molecular weight forms; PEN 2; Proteasomal degradation; Transcript variant

Indexed keywords

GAMMA SECRETASE; MEMBRANE PROTEIN; PRESENILIN 1; PROTEASOME; PROTEIN UBIQUILIN 1 TV1; PROTEIN UBIQUILIN 1 TV3; UNCLASSIFIED DRUG;

EID: 79751480230     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2010.01149.x     Document Type: Article
Times cited : (66)

References (45)
  • 1
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases.
    • Selkoe DJ. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 2004;6: 1054-1061.
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 2
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective.
    • Tanzi RE, Bertram L. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 2005;120:545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 4
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the notch signaling pathway in Caenorhabditis elegans embryos.
    • Goutte C, Tsunozaki M, Hale VA, Priess JR. APH-1 is a multipass membrane protein essential for the notch signaling pathway in Caenorhabditis elegans embryos. Proc Natl Acad Sci U S A 2002;99:775-779.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 7
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation.
    • Mah AL, Perry G, Smith MA, Monteiro MJ. Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J Cell Biol 2000;151:847-862.
    • (2000) J Cell Biol , vol.151 , pp. 847-862
    • Mah, A.L.1    Perry, G.2    Smith, M.A.3    Monteiro, M.J.4
  • 8
    • 27744468749 scopus 로고    scopus 로고
    • Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, pen-2 and nicastrin.
    • Massey LK, Mah AL, Monteiro MJ. Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, pen-2 and nicastrin. Biochem J 2005;391:513-525.
    • (2005) Biochem J , vol.391 , pp. 513-525
    • Massey, L.K.1    Mah, A.L.2    Monteiro, M.J.3
  • 9
    • 33748746862 scopus 로고    scopus 로고
    • Interaction between presenilin 1 and ubiquilin 1 as detected by fluorescence lifetime imaging microscopy and a high-throughput fluorescent plate reader.
    • Thomas AV, Herl L, Spoelgen R, Hiltunen M, Jones PB, Tanzi RE, Hyman BT, Berezovska O. Interaction between presenilin 1 and ubiquilin 1 as detected by fluorescence lifetime imaging microscopy and a high-throughput fluorescent plate reader. J Biol Chem 2006;281:26400-26407.
    • (2006) J Biol Chem , vol.281 , pp. 26400-26407
    • Thomas, A.V.1    Herl, L.2    Spoelgen, R.3    Hiltunen, M.4    Jones, P.B.5    Tanzi, R.E.6    Hyman, B.T.7    Berezovska, O.8
  • 12
    • 35448970692 scopus 로고    scopus 로고
    • Isolation and characterization of the Drosophila ubiquilin ortholog dUbqln: in vivo interaction with early-onsheimer disease genes.
    • Li A, Xie Z, Dong Y, McKay KM, McKee ML, Tanzi RE. Isolation and characterization of the Drosophila ubiquilin ortholog dUbqln: in vivo interaction with early-onset Alzheimer disease genes. Hum Mol Genet 2007;16:2626-2639.
    • (2007) Hum Mol Genet , vol.16 , pp. 2626-2639
    • Li, A.1    Xie, Z.2    Dong, Y.3    McKay, K.M.4    McKee, M.L.5    Tanzi, R.E.6
  • 13
    • 2442520399 scopus 로고    scopus 로고
    • Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains.
    • Ko HS, Uehara T, Tsuruma K, Nomura Y. Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains. FEBS Lett 2004;566:110-114.
    • (2004) FEBS Lett , vol.566 , pp. 110-114
    • Ko, H.S.1    Uehara, T.2    Tsuruma, K.3    Nomura, Y.4
  • 14
    • 0033568315 scopus 로고    scopus 로고
    • Identification of XDRP1; a xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation.
    • Funakoshi M, Geley S, Hunt T, Nishimoto T, Kobayashi H. Identification of XDRP1; a xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation. EMBO J 1999;18:5009-5018.
    • (1999) EMBO J , vol.18 , pp. 5009-5018
    • Funakoshi, M.1    Geley, S.2    Hunt, T.3    Nishimoto, T.4    Kobayashi, H.5
  • 16
    • 0037378613 scopus 로고    scopus 로고
    • Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase.
    • Gao L, Tu H, Shi ST, Lee KJ, Asanaka M, Hwang SB, Lai MM. Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase. J Virol 2003;77:4149-4159.
    • (2003) J Virol , vol.77 , pp. 4149-4159
    • Gao, L.1    Tu, H.2    Shi, S.T.3    Lee, K.J.4    Asanaka, M.5    Hwang, S.B.6    Lai, M.M.7
  • 18
    • 0141632772 scopus 로고    scopus 로고
    • The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome.
    • Kleijnen MF, Alarcon RM, Howley PM. The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Mol Biol Cell 2003;14:3868-3875.
    • (2003) Mol Biol Cell , vol.14 , pp. 3868-3875
    • Kleijnen, M.F.1    Alarcon, R.M.2    Howley, P.M.3
  • 21
    • 65549084887 scopus 로고    scopus 로고
    • Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1.
    • Kim SH, Shi Y, Hanson KA, Williams LM, Sakasai R, Bowler MJ, Tibbetts RS. Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1. J Biol Chem 2009;284:8083-8092.
    • (2009) J Biol Chem , vol.284 , pp. 8083-8092
    • Kim, S.H.1    Shi, Y.2    Hanson, K.A.3    Williams, L.M.4    Sakasai, R.5    Bowler, M.J.6    Tibbetts, R.S.7
  • 22
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation.
    • N'Diaye EN, Kajihara KK, Hsieh I, Morisaki H, Debnath J, Brown EJ. PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation. EMBO Rep 2009;10:173-179.
    • (2009) EMBO Rep , vol.10 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6
  • 23
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation.
    • Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000;10:524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 24
    • 39049148153 scopus 로고    scopus 로고
    • Aggresome formation and neurodegenerative diseases: therapeutic implications.
    • Olzmann JA, Li L, Chin LS. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr Med Chem 2008;15:47-60.
    • (2008) Curr Med Chem , vol.15 , pp. 47-60
    • Olzmann, J.A.1    Li, L.2    Chin, L.S.3
  • 27
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins.
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998;143:1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 28
    • 0036677215 scopus 로고    scopus 로고
    • Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells.
    • Namekata K, Nishimura N, Kimura H. Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells. J Neurochem 2002;82:819-827.
    • (2002) J Neurochem , vol.82 , pp. 819-827
    • Namekata, K.1    Nishimura, N.2    Kimura, H.3
  • 29
    • 71749094769 scopus 로고    scopus 로고
    • Down-regulation of seladin-1 increases BACE1 levels and activity through enhanced GGA3 depletion during apoptosis.
    • Sarajarvi T, Haapasalo A, Viswanathan J, Makinen P, Laitinen M, Soininen H, Hiltunen M. Down-regulation of seladin-1 increases BACE1 levels and activity through enhanced GGA3 depletion during apoptosis. J Biol Chem 2009;284:34433-34443.
    • (2009) J Biol Chem , vol.284 , pp. 34433-34443
    • Sarajarvi, T.1    Haapasalo, A.2    Viswanathan, J.3    Makinen, P.4    Laitinen, M.5    Soininen, H.6    Hiltunen, M.7
  • 31
    • 34547640864 scopus 로고    scopus 로고
    • Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2.
    • Ford DL, Monteiro MJ. Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2. Biochemistry 2007;46:8827-8837.
    • (2007) Biochemistry , vol.46 , pp. 8827-8837
    • Ford, D.L.1    Monteiro, M.J.2
  • 34
    • 65549099222 scopus 로고    scopus 로고
    • All-you-can-eat: autophagy in neurodegeneration and neuroprotection.
    • Jaeger PA, Wyss-Coray T. All-you-can-eat: autophagy in neurodegeneration and neuroprotection. Mol Neurodegeneration 2009;4:16.
    • (2009) Mol Neurodegeneration , vol.4 , pp. 16
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 35
    • 33744954445 scopus 로고    scopus 로고
    • Presenilin 1 forms aggresomal deposits in response to heat shock.
    • Kovacs I, Lentini KM, Ingano LM, Kovacs DM. Presenilin 1 forms aggresomal deposits in response to heat shock. J Mol Neurosci 2006;29:9-19.
    • (2006) J Mol Neurosci , vol.29 , pp. 9-19
    • Kovacs, I.1    Lentini, K.M.2    Ingano, L.M.3    Kovacs, D.M.4
  • 37
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates.
    • Doi H, Mitsui K, Kurosawa M, Machida Y, Kuroiwa Y, Nukina N. Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett 2004;571:171-176.
    • (2004) FEBS Lett , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 41
  • 42
    • 24644460177 scopus 로고    scopus 로고
    • Enhanced caffeine-induced Ca2+ release in the 3xTg-AD mouse model of Alzheimer's disease.
    • Smith IF, Hitt B, Green KN, Oddo S, LaFerla FM. Enhanced caffeine-induced Ca2+ release in the 3xTg-AD mouse model of Alzheimer's disease. J Neurochem 2005;94:1711-1718.
    • (2005) J Neurochem , vol.94 , pp. 1711-1718
    • Smith, I.F.1    Hitt, B.2    Green, K.N.3    Oddo, S.4    LaFerla, F.M.5
  • 43
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity.
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999;398:513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.