메뉴 건너뛰기




Volumn 17, Issue 11, 2008, Pages 1540-1555

Autophagy induced by Alexander disease-mutant GFAP accumulation is regulated by p38/MAPK and mTOR signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

GLIAL FIBRILLARY ACIDIC PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE P38; SYNAPTOPHYSIN;

EID: 44349107112     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddn042     Document Type: Article
Times cited : (147)

References (46)
  • 1
    • 0023881165 scopus 로고
    • Isolation of a major protein component of Rosenthal fibers
    • Goldman, J.E. and Corbin, L. (1966) Isolation of a major protein component of Rosenthal fibers. Am. J. Pathol., 130, 569-578.
    • (1966) Am. J. Pathol , vol.130 , pp. 569-578
    • Goldman, J.E.1    Corbin, L.2
  • 2
    • 0027724243 scopus 로고
    • Overexpression and abnormal modification of the stress protein alplha B-crystallin and HSP27 in Alexander disease
    • Head, M.W., Corbin, E. and Goldman, J.E. (1993) Overexpression and abnormal modification of the stress protein alplha B-crystallin and HSP27 in Alexander disease. Am. J. Pathol., 143, 1743-1753.
    • (1993) Am. J. Pathol , vol.143 , pp. 1743-1753
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 3
    • 0035163913 scopus 로고    scopus 로고
    • Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease
    • Brenner, M., Johnson, A.B., Boespflug-Tanguy, O., Rodriguez, D., Goldman, J.E. and Messing, A. (2001) Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nat. Genet., 27, 117-120.
    • (2001) Nat. Genet , vol.27 , pp. 117-120
    • Brenner, M.1    Johnson, A.B.2    Boespflug-Tanguy, O.3    Rodriguez, D.4    Goldman, J.E.5    Messing, A.6
  • 4
    • 3142748164 scopus 로고    scopus 로고
    • Alexander disease: A leukodystrophy caused by a mutation in GFAP
    • Johnson, A.B. (2004) Alexander disease: A leukodystrophy caused by a mutation in GFAP. Neurochem. Res., 29, 961-964.
    • (2004) Neurochem. Res , vol.29 , pp. 961-964
    • Johnson, A.B.1
  • 8
    • 19444366359 scopus 로고    scopus 로고
    • Alexander-disease mutation of GFAP causes filament disomanization and decreased solubility of GFAP
    • Hsiao, V.C., Tian, R., Long, H., Der Perng, M., Brenner, M., Quinlan, R.A. and Goldman, J.E. (2005) Alexander-disease mutation of GFAP causes filament disomanization and decreased solubility of GFAP. J. Cell Sci., 118,
    • (2005) J. Cell Sci , vol.118
    • Hsiao, V.C.1    Tian, R.2    Long, H.3    Der Perng, M.4    Brenner, M.5    Quinlan, R.A.6    Goldman, J.E.7
  • 9
    • 0032956263 scopus 로고    scopus 로고
    • Formation of GFAP cvtoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin
    • Kovama, Y. and Goldman, J.E. (1999) Formation of GFAP cvtoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin Am. J. Pathol., 154, 1563-1572.
    • (1999) Am. J. Pathol , vol.154 , pp. 1563-1572
    • Kovama, Y.1    Goldman, J.E.2
  • 10
    • 33846002775 scopus 로고    scopus 로고
    • Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease
    • Tang, G., Xu, Z. and Goldman, J.E. (2006) Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease. J. Biol. Chem., 281 38634-38643.
    • (2006) J. Biol. Chem , vol.281 , pp. 38634-38643
    • Tang, G.1    Xu, Z.2    Goldman, J.E.3
  • 11
    • 33644642950 scopus 로고    scopus 로고
    • Plectin regulate the organization of glial fibrillary acidic protein in Alexander disease
    • Tian, R., Gregor, M., Wiche, G. and Goldman, J.E. (2006) Plectin regulate the organization of glial fibrillary acidic protein in Alexander disease. Am. J. Pathol., 168, 888-897.
    • (2006) Am. J. Pathol , vol.168 , pp. 888-897
    • Tian, R.1    Gregor, M.2    Wiche, G.3    Goldman, J.E.4
  • 12
    • 3042723794 scopus 로고    scopus 로고
    • Autophagy: Molecular mechanism, physiological functions and relevance in human pathology
    • Marino, G. and Lopez-Otin, C. (2004) Autophagy: Molecular mechanism, physiological functions and relevance in human pathology. Cell Mol. Life Sci., 61, 1439-1454
    • (2004) Cell Mol. Life Sci , vol.61 , pp. 1439-1454
    • Marino, G.1    Lopez-Otin, C.2
  • 13
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout, H.J., Lang-Rollin, I. and Stefanis, L. (2004) Involvement of macroautophagy in the dissolution of neuronal inclusions. Int. J. Biochem. Cell Biol., 36, 2551-2562.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 15
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a flourescent autophagosome marker
    • Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T. and Ohsumi, Y. (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a flourescent autophagosome marker. Mol. Biol. Cell, 15, 1101-1111.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 16
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblotting
    • Mizushima, N., and Yoshimori, T. (2007) How to interpret LC3 immunoblotting. Autophagy, 3, 542-545.
    • (2007) Autophagy , vol.3 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 17
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., StenmarK, H. and Johansen, T. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol., 171, 603-614.
    • (2005) J. Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    StenmarK, H.7    Johansen, T.8
  • 20
    • 33751073409 scopus 로고    scopus 로고
    • Alexander disease-associated glial fibrillary acidic protein mutations in mice induce Rosenthal fiber formation and a white matter stress response
    • Hagemann, T.L., Connor, J.X., and Messing, A. (2006) Alexander disease-associated glial fibrillary acidic protein mutations in mice induce Rosenthal fiber formation and a white matter stress response. J. Neurosci., 26, 11162-11173.
    • (2006) J. Neurosci , vol.26 , pp. 11162-11173
    • Hagemann, T.L.1    Connor, J.X.2    Messing, A.3
  • 21
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R. and Rubinsztein, D.C. (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet., 11, 1107-1117.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 24
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto, A., Cremona, M.L. and Rothman, J.E. (2006) Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol., 172, 719-731.
    • (2006) J. Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 25
    • 15444362044 scopus 로고    scopus 로고
    • The stress-inducted protains RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway
    • Corradetti, M.N., Inoki, K. and Guan, K.L. 2005 The stress-inducted protains RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway. J. Biol. Chem., 280, 9769-9772.
    • (2005) J. Biol. Chem , vol.280 , pp. 9769-9772
    • Corradetti, M.N.1    Inoki, K.2    Guan, K.L.3
  • 27
    • 17644373073 scopus 로고    scopus 로고
    • Role of MLK3 in the regulation of mitogen-activated protein kinase signaling cascades
    • Brancho, D., Ventura, J.J., Jaeschke, A., Doran, B., Flavell, R.A. and Davis, R.J. 2005 Role of MLK3 in the regulation of mitogen-activated protein kinase signaling cascades. Mol. Cell Biol., 25, 3670-3681.
    • (2005) Mol. Cell Biol , vol.25 , pp. 3670-3681
    • Brancho, D.1    Ventura, J.J.2    Jaeschke, A.3    Doran, B.4    Flavell, R.A.5    Davis, R.J.6
  • 29
    • 32944460806 scopus 로고    scopus 로고
    • In yeast, loss of Hogl leads to osmosensitivity of autophagy
    • Prick, T., Thumm, M., Kohrer, K., Haussinger, D. and Vom Dahl, S. (2006) In yeast, loss of Hogl leads to osmosensitivity of autophagy. Biochem. J., 394, 153-161.
    • (2006) Biochem. J , vol.394 , pp. 153-161
    • Prick, T.1    Thumm, M.2    Kohrer, K.3    Haussinger, D.4    Vom Dahl, S.5
  • 30
    • 0035865679 scopus 로고    scopus 로고
    • Cell hydration controls autophagosome formation in rat liver in a microtubule-dependent way downstream from p38MAPK activation
    • vom Dahl, S., Dombrowski, F., Schmitt, M., Schliess, F., Pfeifer, U. and Haussinger, D. (2001) Cell hydration controls autophagosome formation in rat liver in a microtubule-dependent way downstream from p38MAPK activation. Biochem. J., 354, 31-36.
    • (2001) Biochem. J , vol.354 , pp. 31-36
    • vom Dahl, S.1    Dombrowski, F.2    Schmitt, M.3    Schliess, F.4    Pfeifer, U.5    Haussinger, D.6
  • 31
    • 0030051528 scopus 로고    scopus 로고
    • MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway
    • Raingeaud, J., Whitmarsh, A.J., Barrett, T., Derijard, B. and Davis, R.J. (1996) MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell Biol., 16, 1247-1255.
    • (1996) Mol. Cell Biol , vol.16 , pp. 1247-1255
    • Raingeaud, J.1    Whitmarsh, A.J.2    Barrett, T.3    Derijard, B.4    Davis, R.J.5
  • 33
    • 5444231258 scopus 로고    scopus 로고
    • Huntington processing in pathogenesis of Huntington disease
    • Qin, Z.H. and Gu, Z.L. (2004) Huntington processing in pathogenesis of Huntington disease. Acta Pharmacol. Sin., 25, 1243-1249.
    • (2004) Acta Pharmacol. Sin , vol.25 , pp. 1243-1249
    • Qin, Z.H.1    Gu, Z.L.2
  • 35
    • 0021324601 scopus 로고
    • Synthesis and turnover of cytoskeletal proteins in cultured astrocytes
    • Chiu, F.C. and Goldman, J.E. (1984) Synthesis and turnover of cytoskeletal proteins in cultured astrocytes. J. Neurochem., 42 166-174.
    • (1984) J. Neurochem , vol.42 , pp. 166-174
    • Chiu, F.C.1    Goldman, J.E.2
  • 37
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D.C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 38
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated hungtintin
    • Iwata, A., Riley, B.E., Johnston, J.A. and Kopito, R.R. (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated hungtintin. J. Biol. Chem., 280, 40282-40292.
    • (2005) J. Biol. Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 39
    • 0034683568 scopus 로고    scopus 로고
    • Tor-mediated induction of autophagy via an Apg1 protein kinase complex
    • Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M. and Ohsumi, Y. (2000) Tor-mediated induction of autophagy via an Apg1 protein kinase complex. J. Cell Biol., 150, 1507-1513.
    • (2000) J. Cell Biol , vol.150 , pp. 1507-1513
    • Kamada, Y.1    Funakoshi, T.2    Shintani, T.3    Nagano, K.4    Ohsumi, M.5    Ohsumi, Y.6
  • 41
    • 0035793574 scopus 로고    scopus 로고
    • p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • Rane, M.J., Coxon, P.Y., Powell, D.W., Webster, R., Klein, J.B., Pierce, W., Ping, P. and McLeish, K.R. (2001) p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J. Biol Chem., 276, 3517-3523.
    • (2001) J. Biol Chem , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3    Webster, R.4    Klein, J.B.5    Pierce, W.6    Ping, P.7    McLeish, K.R.8
  • 43
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and p-mTOR pathways in cells
    • Feng, Z., Zhang, H., Levine, A.J. and Jin, S. (2005) The coordinate regulation of the p53 and p-mTOR pathways in cells. Proc. Natl Acad. Sci., USA, 102, 8204-8209.
    • (2005) Proc. Natl Acad. Sci., USA , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3    Jin, S.4
  • 45
    • 23344432914 scopus 로고    scopus 로고
    • Role of molecular chaperones in neurodegenerative disorders
    • Meriin, A.B. and Sherman, M.Y. (2005) Role of molecular chaperones in neurodegenerative disorders. Int. J. Hyperthermia., 21, 403-419.
    • (2005) Int. J. Hyperthermia , vol.21 , pp. 403-419
    • Meriin, A.B.1    Sherman, M.Y.2
  • 46
    • 0021191576 scopus 로고
    • The role of increased proteolysis in the atrophy and arrest of proliferation in serum-deprived fibroblasts
    • Gronostajski, R.M., Goldberg, A.L. and Pardee, A.B. 1984 The role of increased proteolysis in the atrophy and arrest of proliferation in serum-deprived fibroblasts. J. Cell Physiol., 121, 189-198.
    • (1984) J. Cell Physiol , vol.121 , pp. 189-198
    • Gronostajski, R.M.1    Goldberg, A.L.2    Pardee, A.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.