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Volumn 317, Issue 8, 2011, Pages 1093-1107

Recruitment of APPL1 to ubiquitin-rich aggresomes in response to proteasomal impairment

Author keywords

Aggresome; APPL1; Endosome; Proteasome; Ubiquitination

Indexed keywords

ADAPTOR PROTEIN; CELL PROTEIN; LYSINE; PROTEIN APPL1; PROTEOME; UBIQUITIN; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; VIMENTIN;

EID: 79953069853     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2011.02.002     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 74749099537 scopus 로고    scopus 로고
    • The early endosome: a busy sorting station for proteins at the crossroads
    • Jovic M., Sharma M., Rahajeng J., Caplan S. The early endosome: a busy sorting station for proteins at the crossroads. Histol. Histopathol. 2010, 25:99-112.
    • (2010) Histol. Histopathol. , vol.25 , pp. 99-112
    • Jovic, M.1    Sharma, M.2    Rahajeng, J.3    Caplan, S.4
  • 3
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • Zoncu R., Perera R.M., Balkin D.M., Pirruccello M., Toomre D., De Camilli P. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell 2009, 136:1110-1121.
    • (2009) Cell , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6
  • 4
    • 67349237981 scopus 로고    scopus 로고
    • Ubiquitin in trafficking: the network at work
    • Acconcia F., Sigismund S., Polo S. Ubiquitin in trafficking: the network at work. Exp. Cell Res. 2009, 315:1610-1618.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1610-1618
    • Acconcia, F.1    Sigismund, S.2    Polo, S.3
  • 5
    • 32844471837 scopus 로고    scopus 로고
    • Two different stages of epidermal growth factor (EGF) receptor endocytosis are sensitive to free ubiquitin depletion produced by proteasome inhibitor MG132
    • Melikova M.S., Kondratov K.A., Kornilova E.S. Two different stages of epidermal growth factor (EGF) receptor endocytosis are sensitive to free ubiquitin depletion produced by proteasome inhibitor MG132. Cell Biol. Int. 2006, 30:31-43.
    • (2006) Cell Biol. Int. , vol.30 , pp. 31-43
    • Melikova, M.S.1    Kondratov, K.A.2    Kornilova, E.S.3
  • 6
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva K.E., Blystad F.D., Stang E., Larsen A.M., Johannessen L.E., Madshus I.H. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 2002, 156:843-854.
    • (2002) J. Cell Biol. , vol.156 , pp. 843-854
    • Longva, K.E.1    Blystad, F.D.2    Stang, E.3    Larsen, A.M.4    Johannessen, L.E.5    Madshus, I.H.6
  • 8
    • 0035159679 scopus 로고    scopus 로고
    • Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins
    • van Kerkhof P., Alves dos Santos C.M., Sachse M., Klumperman J., Bu G., Strous G.J. Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins. Mol. Biol. Cell 2001, 12:2556-2566.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2556-2566
    • van Kerkhof, P.1    Alves dos Santos, C.M.2    Sachse, M.3    Klumperman, J.4    Bu, G.5    Strous, G.J.6
  • 10
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori S., Tanaka K., Omura S., Saito Y. Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway. J. Biol. Chem. 1995, 270:29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 11
    • 0031045984 scopus 로고    scopus 로고
    • Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway
    • Jeffers M., Taylor G.A., Weidner K.M., Omura S., Vande Woude G.F. Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell. Biol. 1997, 17:799-808.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 799-808
    • Jeffers, M.1    Taylor, G.A.2    Weidner, K.M.3    Omura, S.4    Vande Woude, G.F.5
  • 12
    • 0035808301 scopus 로고    scopus 로고
    • The proteasome regulates receptor-mediated endocytosis of interleukin-2
    • Yu A., Malek T.R. The proteasome regulates receptor-mediated endocytosis of interleukin-2. J. Biol. Chem. 2001, 276:381-385.
    • (2001) J. Biol. Chem. , vol.276 , pp. 381-385
    • Yu, A.1    Malek, T.R.2
  • 13
    • 42949092018 scopus 로고    scopus 로고
    • The endosomal protein App l1 mediates Akt substrate specificity and cell survival in vertebrate development
    • Schenck A., Goto-Silva L., Collinet C., Rhinn M., Giner A., Habermann B., Brand M., Zerial M. The endosomal protein App l1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell 2008, 133:486-497.
    • (2008) Cell , vol.133 , pp. 486-497
    • Schenck, A.1    Goto-Silva, L.2    Collinet, C.3    Rhinn, M.4    Giner, A.5    Habermann, B.6    Brand, M.7    Zerial, M.8
  • 15
    • 67650540827 scopus 로고    scopus 로고
    • Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-catenin/TCF-mediated transcription
    • Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M. Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-catenin/TCF-mediated transcription. J. Biol. Chem. 2009, 284:18115-18128.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18115-18128
    • Rashid, S.1    Pilecka, I.2    Torun, A.3    Olchowik, M.4    Bielinska, B.5    Miaczynska, M.6
  • 16
    • 70350088552 scopus 로고    scopus 로고
    • Functional characterization of the interactions between endosomal adaptor protein APPL1 and the NuRD co-repressor complex
    • Banach-Orlowska M., Pilecka I., Torun A., Pyrzynska B., Miaczynska M. Functional characterization of the interactions between endosomal adaptor protein APPL1 and the NuRD co-repressor complex. Biochem. J. 2009, 423:389-400.
    • (2009) Biochem. J. , vol.423 , pp. 389-400
    • Banach-Orlowska, M.1    Pilecka, I.2    Torun, A.3    Pyrzynska, B.4    Miaczynska, M.5
  • 17
    • 68249153842 scopus 로고    scopus 로고
    • The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH
    • Han Y.H., Moon H.J., You B.R., Park W.H. The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH. Oncol. Rep. 2009, 22:215-221.
    • (2009) Oncol. Rep. , vol.22 , pp. 215-221
    • Han, Y.H.1    Moon, H.J.2    You, B.R.3    Park, W.H.4
  • 18
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik C., Schroeter D., Wilk S., Lamprecht J., Paweletz N. Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur. J. Cell Biol. 1996, 71:311-318.
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 311-318
    • Wojcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 19
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston J.A., Ward C.L., Kopito R.R. 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
  • 20
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: aggravating aggresomes
    • Garcia-Mata R., Gao Y.S., Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 2002, 3:388-396.
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 21
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. 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
  • 25
    • 0034698787 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis
    • Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P. Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis. J. Cell Biol. 2000, 150:905-912.
    • (2000) J. Cell Biol. , vol.150 , pp. 905-912
    • Confalonieri, S.1    Salcini, A.E.2    Puri, C.3    Tacchetti, C.4    Di Fiore, P.P.5
  • 26
    • 23644436824 scopus 로고    scopus 로고
    • protocol, Calcium phosphate-mediated transfection of eukaryotic cells, Nature Methods 2 (2005) 319-320.
    • protocol, Calcium phosphate-mediated transfection of eukaryotic cells, Nature Methods 2 (2005) 319-320.
  • 28
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J., Ghigo E., Kalaidzidis Y., Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 2005, 122:735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 29
    • 66149146607 scopus 로고    scopus 로고
    • Bortezomib: a review of its use in patients with multiple myeloma
    • Curran M.P., McKeage K. Bortezomib: a review of its use in patients with multiple myeloma. Drugs 2009, 69:859-888.
    • (2009) Drugs , vol.69 , pp. 859-888
    • Curran, M.P.1    McKeage, K.2
  • 30
    • 43049115407 scopus 로고    scopus 로고
    • Bortezomib in mantle cell lymphoma
    • Suh K.S., Goy A. Bortezomib in mantle cell lymphoma. Future Oncol. 2008, 4:149-168.
    • (2008) Future Oncol. , vol.4 , pp. 149-168
    • Suh, K.S.1    Goy, A.2
  • 31
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes in Schwann cells
    • Fortun J., Dunn W.A., Joy S., Li J., Notterpek L. Emerging role for autophagy in the removal of aggresomes in Schwann cells. J. Neurosci. 2003, 23:10672-10680.
    • (2003) J. Neurosci. , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn, W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 33
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R., Bebok Z., Sorscher E.J., Sztul E.S. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 1999, 146:1239-1254.
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 36
    • 38049014824 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway
    • Olzmann J.A., Chin L.S. Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway. Autophagy 2008, 4:85-87.
    • (2008) Autophagy , vol.4 , pp. 85-87
    • Olzmann, J.A.1    Chin, L.S.2
  • 37
    • 36248989248 scopus 로고    scopus 로고
    • The Nedd4-like family of E3 ubiquitin ligases and cancer
    • Chen C., Matesic L.E. The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev. 2007, 26:587-604.
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 587-604
    • Chen, C.1    Matesic, L.E.2
  • 39
    • 10044252090 scopus 로고    scopus 로고
    • Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes
    • Markossian K.A., Kurganov B.I. Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes. Biochem. Mosc 2004, 69:971-984.
    • (2004) Biochem. Mosc , vol.69 , pp. 971-984
    • Markossian, K.A.1    Kurganov, B.I.2
  • 40
    • 33344456519 scopus 로고    scopus 로고
    • Parkin-mediated lysine 63-linked polyubiquitination: a link to protein inclusions formation in Parkinson's and other conformational diseases?
    • Lim K.L., Dawson V.L., Dawson T.M. Parkin-mediated lysine 63-linked polyubiquitination: a link to protein inclusions formation in Parkinson's and other conformational diseases?. Neurobiol. Aging 2006, 27:524-529.
    • (2006) Neurobiol. Aging , vol.27 , pp. 524-529
    • Lim, K.L.1    Dawson, V.L.2    Dawson, T.M.3
  • 41
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A., Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003, 40:427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.