메뉴 건너뛰기




Volumn 35, Issue 10, 2014, Pages 2394-2403

The lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies

Author keywords

Dementia; ER associated degradation; Neuropathology; Neuroserpin; Proteasome; Proteostasis

Indexed keywords

GLYCAN; LECTIN; NEUROSERPIN; NEUROPEPTIDE; OS9 PROTEIN, HUMAN; POLYSACCHARIDE; PROTEASOME; PROTEIN BINDING; SERINE PROTEINASE INHIBITOR; TUMOR PROTEIN; UBIQUITIN;

EID: 84903815342     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2014.04.002     Document Type: Article
Times cited : (23)

References (51)
  • 4
    • 76149098224 scopus 로고    scopus 로고
    • Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
    • Bernasconi R., Galli C., Calanca V., Nakajima T., Molinari M. Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. J.Cell Biol. 2010, 188:223-235.
    • (2010) J.Cell Biol. , vol.188 , pp. 223-235
    • Bernasconi, R.1    Galli, C.2    Calanca, V.3    Nakajima, T.4    Molinari, M.5
  • 5
    • 47749109897 scopus 로고    scopus 로고
    • Adual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal
    • Bernasconi R., Pertel T., Luban J., Molinari M. Adual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J.Biol. Chem. 2008, 283:16446-16454.
    • (2008) J.Biol. Chem. , vol.283 , pp. 16446-16454
    • Bernasconi, R.1    Pertel, T.2    Luban, J.3    Molinari, M.4
  • 6
    • 0035823216 scopus 로고    scopus 로고
    • Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease
    • Briand C., Kozlov S.V., Sonderegger P., Grutter M.G. Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease. FEBS Lett. 2001, 505:18-22.
    • (2001) FEBS Lett. , vol.505 , pp. 18-22
    • Briand, C.1    Kozlov, S.V.2    Sonderegger, P.3    Grutter, M.G.4
  • 7
    • 27744542188 scopus 로고    scopus 로고
    • Cell toxicity and conformational disease
    • Carrell R.W. Cell toxicity and conformational disease. Trends Cell Biol. 2005, 15:574-580.
    • (2005) Trends Cell Biol. , vol.15 , pp. 574-580
    • Carrell, R.W.1
  • 8
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., Lomas D.A. Conformational disease. Lancet 1997, 350:134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 9
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10:272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 12
    • 67650526104 scopus 로고    scopus 로고
    • Neuroserpin polymers activate NF-{kappa}B by a calcium signaling pathway that is independent of the unfolded protein response
    • Davies M.J., Miranda E., Roussel B.D., Kaufman R.J., Marciniak S.J., Lomas D.A. Neuroserpin polymers activate NF-{kappa}B by a calcium signaling pathway that is independent of the unfolded protein response. J.Biol. Chem. 2009, 284:18202-18209.
    • (2009) J.Biol. Chem. , vol.284 , pp. 18202-18209
    • Davies, M.J.1    Miranda, E.2    Roussel, B.D.3    Kaufman, R.J.4    Marciniak, S.J.5    Lomas, D.A.6
  • 16
    • 34247877700 scopus 로고    scopus 로고
    • Accumulation of mutant neuroserpin precedes development of clinical symptoms in familial encephalopathy with neuroserpin inclusion bodies
    • Galliciotti G., Glatzel M., Kinter J., Kozlov V.K., Cinelli P., Rülicke T., Sonderegger P. Accumulation of mutant neuroserpin precedes development of clinical symptoms in familial encephalopathy with neuroserpin inclusion bodies. Am. J. Pathol. 2007, 170:1305-1313.
    • (2007) Am. J. Pathol. , vol.170 , pp. 1305-1313
    • Galliciotti, G.1    Glatzel, M.2    Kinter, J.3    Kozlov, V.K.4    Cinelli, P.5    Rülicke, T.6    Sonderegger, P.7
  • 17
    • 0034891027 scopus 로고    scopus 로고
    • Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion
    • Glatzel M., Heppner F.L., Albers K.M., Aguzzi A. Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion. Neuron 2001, 31:25-34.
    • (2001) Neuron , vol.31 , pp. 25-34
    • Glatzel, M.1    Heppner, F.L.2    Albers, K.M.3    Aguzzi, A.4
  • 18
    • 69249124617 scopus 로고    scopus 로고
    • Mechanisms of emphysema in alpha1-antitrypsin deficiency: molecular and cellular insights
    • Gooptu B., Ekeowa U.I., Lomas D.A. Mechanisms of emphysema in alpha1-antitrypsin deficiency: molecular and cellular insights. Eur. Respir. J. 2009, 34:475-488.
    • (2009) Eur. Respir. J. , vol.34 , pp. 475-488
    • Gooptu, B.1    Ekeowa, U.I.2    Lomas, D.A.3
  • 19
    • 78651394090 scopus 로고    scopus 로고
    • Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps
    • Groisman B., Shenkman M., Ron E., Lederkremer G.Z. Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. J.Biol. Chem. 2011, 286:1292-1300.
    • (2011) J.Biol. Chem. , vol.286 , pp. 1292-1300
    • Groisman, B.1    Shenkman, M.2    Ron, E.3    Lederkremer, G.Z.4
  • 20
    • 80052033433 scopus 로고    scopus 로고
    • Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 gene
    • Hagen M.C., Murrell J.R., Delisle M.B., Andermann E., Andermann F., Guiot M.C., Ghetti B. Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 gene. Brain Pathol. 2011, 21:575-582.
    • (2011) Brain Pathol. , vol.21 , pp. 575-582
    • Hagen, M.C.1    Murrell, J.R.2    Delisle, M.B.3    Andermann, E.4    Andermann, F.5    Guiot, M.C.6    Ghetti, B.7
  • 21
    • 0031452755 scopus 로고    scopus 로고
    • Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival
    • Hastings G.A., Coleman T.A., Haudenschild C.C., Stefansson S., Smith E.P., Barthlow R., Cherry S., Sandkvist M., Lawrence D.A. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. J.Biol. Chem. 1997, 272:33062-33067.
    • (1997) J.Biol. Chem. , vol.272 , pp. 33062-33067
    • Hastings, G.A.1    Coleman, T.A.2    Haudenschild, C.C.3    Stefansson, S.4    Smith, E.P.5    Barthlow, R.6    Cherry, S.7    Sandkvist, M.8    Lawrence, D.A.9
  • 22
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J.Biol. Chem. 2009, 284:17061-17068.
    • (2009) J.Biol. Chem. , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 23
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold withthe HRD1-SEL1L ubiquitin ligase complex and BiP
    • Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K. Human XTP3-B forms an endoplasmic reticulum quality control scaffold withthe HRD1-SEL1L ubiquitin ligase complex and BiP. J.Biol. Chem. 2008, 283:20914-20924.
    • (2008) J.Biol. Chem. , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 24
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M., Walker L.C. Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann. Neurol. 2011, 70:532-540.
    • (2011) Ann. Neurol. , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 25
    • 84856323688 scopus 로고    scopus 로고
    • Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    • Kriegenburg F., Ellgaard L., Hartmann-Petersen R. Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J. 2012, 279:532-542.
    • (2012) FEBS J. , vol.279 , pp. 532-542
    • Kriegenburg, F.1    Ellgaard, L.2    Hartmann-Petersen, R.3
  • 26
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • Kroeger H., Miranda E., Macleod I., Perez J., Crowther D.C., Marciniak S.J., Lomas D.A. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J.Biol. Chem. 2009, 21:22793-22802.
    • (2009) J.Biol. Chem. , vol.21 , pp. 22793-22802
    • Kroeger, H.1    Miranda, E.2    Macleod, I.3    Perez, J.4    Crowther, D.C.5    Marciniak, S.J.6    Lomas, D.A.7
  • 27
    • 0030690117 scopus 로고    scopus 로고
    • Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse
    • Krueger S.R., Ghisu G.P., Cinelli P., Gschwend T.P., Osterwalder T., Wolfer D.P., Sonderegger P. Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse. J.Neurosci. 1997, 17:8984-8996.
    • (1997) J.Neurosci. , vol.17 , pp. 8984-8996
    • Krueger, S.R.1    Ghisu, G.P.2    Cinelli, P.3    Gschwend, T.P.4    Osterwalder, T.5    Wolfer, D.P.6    Sonderegger, P.7
  • 28
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer G.Z. Glycoprotein folding, quality control and ER-associated degradation. Curr. Opin. Struct. Biol. 2009, 19:515-523.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 29
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • Liu Y., Choudhury P., Cabral C.M., Sifers R.N. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J.Biol. Chem. 1999, 274:5861-5867.
    • (1999) J.Biol. Chem. , vol.274 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 30
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas D.A., Carrell R.W. Serpinopathies and the conformational dementias. Nat. Rev. Genet. 2002, 3:759-768.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 33
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • Miranda E., Romisch K., Lomas D.A. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J.Biol. Chem. 2004, 279:28283-28291.
    • (2004) J.Biol. Chem. , vol.279 , pp. 28283-28291
    • Miranda, E.1    Romisch, K.2    Lomas, D.A.3
  • 34
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa K., Huyer G., Michaelis S., Brodsky J.L. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 2008, 132:101-112.
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 36
    • 0031893597 scopus 로고    scopus 로고
    • The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin
    • Osterwalder T., Cinelli P., Baici A., Pennella A., Krueger S.R., Schrimpf S.P., Meins M., Sonderegger P. The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin. J.Biol. Chem. 1998, 273:2312-2321.
    • (1998) J.Biol. Chem. , vol.273 , pp. 2312-2321
    • Osterwalder, T.1    Cinelli, P.2    Baici, A.3    Pennella, A.4    Krueger, S.R.5    Schrimpf, S.P.6    Meins, M.7    Sonderegger, P.8
  • 43
    • 0023907965 scopus 로고
    • Aframeshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum
    • Sifers R.N., Brashears-Macatee S., Kidd V.J., Muensch H., Woo S.L. Aframeshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum. J.Biol. Chem. 1988, 263:7330-7335.
    • (1988) J.Biol. Chem. , vol.263 , pp. 7330-7335
    • Sifers, R.N.1    Brashears-Macatee, S.2    Kidd, V.J.3    Muensch, H.4    Woo, S.L.5
  • 45
    • 58149100036 scopus 로고    scopus 로고
    • Mutation-, aging-, and gene dosage-dependent accumulation of neuroserpin (G392E) in endoplasmic reticula and lysosomes of neurons in transgenic mice
    • Takasawa A., Kato I., Takasawa K., Ishii Y., Yoshida T., Shehata M.H., Kawaguchi H., Mohafez O.M., Sasahara M., Hiraga K. Mutation-, aging-, and gene dosage-dependent accumulation of neuroserpin (G392E) in endoplasmic reticula and lysosomes of neurons in transgenic mice. J.Biol. Chem. 2008, 283:35606-35613.
    • (2008) J.Biol. Chem. , vol.283 , pp. 35606-35613
    • Takasawa, A.1    Kato, I.2    Takasawa, K.3    Ishii, Y.4    Yoshida, T.5    Shehata, M.H.6    Kawaguchi, H.7    Mohafez, O.M.8    Sasahara, M.9    Hiraga, K.10
  • 47
  • 48
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9:944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 49
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki M., Li W., Johnson D.J., Huntington J.A. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 2008, 455:1255-1258.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 50
    • 1642336131 scopus 로고    scopus 로고
    • Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system
    • Yepes M., Lawrence D.A. Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system. Thromb. Haemost. 2004, 91:457-464.
    • (2004) Thromb. Haemost. , vol.91 , pp. 457-464
    • Yepes, M.1    Lawrence, D.A.2
  • 51
    • 79957991349 scopus 로고    scopus 로고
    • The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin
    • Ying Z., Wang H., Fan H., Wang G. The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin. J.Biol. Chem. 2011, 286:20835-20844.
    • (2011) J.Biol. Chem. , vol.286 , pp. 20835-20844
    • Ying, Z.1    Wang, H.2    Fan, H.3    Wang, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.