메뉴 건너뛰기




Volumn 131, Issue 6, 2007, Pages 1149-1163

Homeostatic Levels of p62 Control Cytoplasmic Inclusion Body Formation in Autophagy-Deficient Mice

(25)  Komatsu, Masaaki a,b,c   Waguri, Satoshi d   Koike, Masato e   Sou, Yu shin a,b   Ueno, Takashi b   Hara, Taichi f   Mizushima, Noboru c,f   Iwata, Jun ichi a,b   Ezaki, Junji b   Murata, Shigeo a   Hamazaki, Jun a   Nishito, Yasumasa a   Iemura, Shun ichiro g   Natsume, Tohru g   Yanagawa, Toru h   Uwayama, Junya h   Warabi, Eiji h   Yoshida, Hiroshi h   Ishii, Tetsuro h   Kobayashi, Akira i   more..


Author keywords

CELLBIO; HUMDISEASE; PROTEINS

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN 5; PROTEIN P62;

EID: 36849089101     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.10.035     Document Type: Article
Times cited : (1842)

References (36)
  • 1
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M., Mitra S., Schweitzer E.S., Segal M.R., and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004) 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 2
    • 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. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171 (2005) 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
  • 3
    • 0014032729 scopus 로고
    • Nuclei from rat liver: isolation method that combines purity with high yield
    • Blobel G., and Potter V.R. Nuclei from rat liver: isolation method that combines purity with high yield. Science 154 (1966) 1662-1665
    • (1966) Science , vol.154 , pp. 1662-1665
    • Blobel, G.1    Potter, V.R.2
  • 4
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • Elmore S.P., Qian T., Grissom S.F., and Lemasters J.J. The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J. 15 (2001) 2286-2287
    • (2001) FASEB J. , vol.15 , pp. 2286-2287
    • Elmore, S.P.1    Qian, T.2    Grissom, S.F.3    Lemasters, J.J.4
  • 5
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes in Schwann cells
    • Fortun J., Dunn Jr. W.A., Joy S., Li J., and Notterpek L. Emerging role for autophagy in the removal of aggresomes in Schwann cells. J. Neurosci. 23 (2003) 10672-10680
    • (2003) J. Neurosci. , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn Jr., W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 6
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426 (2003) 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 9
    • 0030582370 scopus 로고    scopus 로고
    • Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in response to oxidative stress
    • Ishii T., Yanagawa T., Kawane T., Yuki K., Seita J., Yoshida H., and Bannai S. Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in response to oxidative stress. Biochem. Biophys. Res. Commun. 226 (1996) 456-460
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 456-460
    • Ishii, T.1    Yanagawa, T.2    Kawane, T.3    Yuki, K.4    Seita, J.5    Yoshida, H.6    Bannai, S.7
  • 12
    • 33645216184 scopus 로고    scopus 로고
    • Intracellular inclusions containing mutant alpha1-antitrypsin Z are propagated in the absence of autophagic activity
    • Kamimoto T., Shoji S., Hidvegi T., Mizushima N., Umebayashi K., Perlmutter D.H., and Yoshimori T. Intracellular inclusions containing mutant alpha1-antitrypsin Z are propagated in the absence of autophagic activity. J. Biol. Chem. 281 (2006) 4467-4476
    • (2006) J. Biol. Chem. , vol.281 , pp. 4467-4476
    • Kamimoto, T.1    Shoji, S.2    Hidvegi, T.3    Mizushima, N.4    Umebayashi, K.5    Perlmutter, D.H.6    Yoshimori, T.7
  • 18
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E., Salminen A., and Alafuzoff I. Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 12 (2001) 2085-2090
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 20
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine B., and Klionsky D.J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6 (2004) 463-477
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 22
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N., Yamamoto A., Matsui M., Yoshimori T., and Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 15 (2004) 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
  • 23
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • Moscat J., Diaz-Meco M.T., Albert A., and Campuzano S. Cell signaling and function organized by PB1 domain interactions. Mol. Cell 23 (2006) 631-640
    • (2006) Mol. Cell , vol.23 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 24
    • 1842789629 scopus 로고    scopus 로고
    • Expression of ubiquitin-binding protein p62 in ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis with dementia: analysis of five autopsy cases with broad clinicopathological spectrum
    • Nakano T., Nakaso K., Nakashima K., and Ohama E. Expression of ubiquitin-binding protein p62 in ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis with dementia: analysis of five autopsy cases with broad clinicopathological spectrum. Acta Neuropathol. (Berl.) 107 (2004) 359-364
    • (2004) Acta Neuropathol. (Berl.) , vol.107 , pp. 359-364
    • Nakano, T.1    Nakaso, K.2    Nakashima, K.3    Ohama, E.4
  • 25
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: two ubiquitin-like systems
    • Ohsumi Y. Molecular dissection of autophagy: two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2 (2001) 211-216
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 28
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross C.A., and Poirier M.A. Opinion: What is the role of protein aggregation in neurodegeneration?. Nat. Rev. Mol. Cell Biol. 6 (2005) 891-898
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 29
    • 0031946369 scopus 로고    scopus 로고
    • Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62
    • Sanchez P., De Carcer G., Sandoval I.V., Moscat J., and Diaz-Meco M.T. Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol. Cell. Biol. 18 (1998) 3069-3080
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3069-3080
    • Sanchez, P.1    De Carcer, G.2    Sandoval, I.V.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 30
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., Mahlke C., and Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421 (2003) 373-379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 33
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism
    • Tong K.I., Kobayashi A., Katsuoka F., and Yamamoto M. Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol. Chem. 387 (2006) 1311-1320
    • (2006) Biol. Chem. , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 34
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M., and Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333 (1993) 169-174
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 36
    • 33746805387 scopus 로고    scopus 로고
    • Signaling, polyubiquitination, trafficking, and inclusions: Sequestosome 1/p62′s role in neurodegenerative disease
    • Wooten M.W., Hu X., Babu J.R., Seibenhener M.L., Geetha T., Paine M.G., and Wooten M.C. Signaling, polyubiquitination, trafficking, and inclusions: Sequestosome 1/p62′s role in neurodegenerative disease. J. Biomed. Biotechnol. 2006 (2006) 62079
    • (2006) J. Biomed. Biotechnol. , vol.2006 , pp. 62079
    • Wooten, M.W.1    Hu, X.2    Babu, J.R.3    Seibenhener, M.L.4    Geetha, T.5    Paine, M.G.6    Wooten, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.