메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages 19-30

The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; REGULATOR PROTEIN; RPN10 PROTEIN; UNCLASSIFIED DRUG;

EID: 84892433922     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.06.006     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 0030805134 scopus 로고    scopus 로고
    • Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26S proteasome
    • Anand G., Yin X., Shahidi A.K., Grove L., Prochownik E.V. Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26S proteasome. J.Biol. Chem. 1997, 272:19140-19151.
    • (1997) J.Biol. Chem. , vol.272 , pp. 19140-19151
    • Anand, G.1    Yin, X.2    Shahidi, A.K.3    Grove, L.4    Prochownik, E.V.5
  • 2
    • 0025238437 scopus 로고
    • The protein Id: a negative regulator of helix-loop-helix DNA binding proteins
    • Benezra R., Davis R.L., Lockshon D., Turner D.L., Weintraub H. The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 1990, 61:49-59.
    • (1990) Cell , vol.61 , pp. 49-59
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 3
    • 67649654465 scopus 로고    scopus 로고
    • Getting to first base in proteasome assembly
    • Besche H.C., Peth A., Goldberg A.L. Getting to first base in proteasome assembly. Cell 2009, 138:25-28.
    • (2009) Cell , vol.138 , pp. 25-28
    • Besche, H.C.1    Peth, A.2    Goldberg, A.L.3
  • 4
    • 76749131595 scopus 로고    scopus 로고
    • Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines
    • Bingol B., Wang C.F., Arnott D., Cheng D., Peng J., Sheng M. Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines. Cell 2010, 140:567-578.
    • (2010) Cell , vol.140 , pp. 567-578
    • Bingol, B.1    Wang, C.F.2    Arnott, D.3    Cheng, D.4    Peng, J.5    Sheng, M.6
  • 5
    • 84856290771 scopus 로고    scopus 로고
    • The centrosome in cells and organisms
    • Bornens M. The centrosome in cells and organisms. Science 2012, 335:422-426.
    • (2012) Science , vol.335 , pp. 422-426
    • Bornens, M.1
  • 7
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma N.P., Lindsten K., Glas R., Jellne M., Masucci M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 2000, 18:538-543.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 9
    • 70350389831 scopus 로고    scopus 로고
    • Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
    • Djakovic S.N., Schwarz L.A., DeMartino G.N., Patrick G.N. Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 2009, 284:26655-26665.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26655-26665
    • Djakovic, S.N.1    Schwarz, L.A.2    DeMartino, G.N.3    Patrick, G.N.4
  • 10
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • Fu H., Reis N., Lee Y., Glickman M.H., Vierstra R.D. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J. 2001, 20:7096-7107.
    • (2001) EMBO J. , vol.20 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 11
    • 1642493720 scopus 로고    scopus 로고
    • A CaMKII-NeuroD signaling pathway specifies dendritic morphogenesis
    • Gaudillière B., Konishi Y., de la Iglesia N., Yao Gl., Bonni A. A CaMKII-NeuroD signaling pathway specifies dendritic morphogenesis. Neuron 2004, 41:229-241.
    • (2004) Neuron , vol.41 , pp. 229-241
    • Gaudillière, B.1    Konishi, Y.2    de la Iglesia, N.3    Yao, G.4    Bonni, A.5
  • 12
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • Gillingham A.K., Munro S. The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep. 2000, 1:524-529.
    • (2000) EMBO Rep. , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 13
    • 77951783385 scopus 로고    scopus 로고
    • The immunological synapse: a focal point for endocytosis and exocytosis
    • Griffiths G.M., Tsun A., Stinchcombe J.C. The immunological synapse: a focal point for endocytosis and exocytosis. J.Cell Biol. 2010, 189:399-406.
    • (2010) J.Cell Biol. , vol.189 , pp. 399-406
    • Griffiths, G.M.1    Tsun, A.2    Stinchcombe, J.C.3
  • 14
    • 40749118584 scopus 로고    scopus 로고
    • Interference of the dominant negative helix-loop-helix protein ID1 with the proteasomal subunit S5A causes centrosomal abnormalities
    • Hasskarl J., Mern D.S., Münger K. Interference of the dominant negative helix-loop-helix protein ID1 with the proteasomal subunit S5A causes centrosomal abnormalities. Oncogene 2008, 27:1657-1664.
    • (2008) Oncogene , vol.27 , pp. 1657-1664
    • Hasskarl, J.1    Mern, D.S.2    Münger, K.3
  • 15
    • 0028956797 scopus 로고
    • Mechanisms of neural patterning and specification in the developing cerebellum
    • Hatten M.E., Heintz N. Mechanisms of neural patterning and specification in the developing cerebellum. Annu. Rev. Neurosci. 1995, 18:385-408.
    • (1995) Annu. Rev. Neurosci. , vol.18 , pp. 385-408
    • Hatten, M.E.1    Heintz, N.2
  • 18
    • 0034675885 scopus 로고    scopus 로고
    • Characterization of the signal that directs Tom20 to the mitochondrial outer membrane
    • Kanaji S., Iwahashi J., Kida Y., Sakaguchi M., Mihara K. Characterization of the signal that directs Tom20 to the mitochondrial outer membrane. J.Cell Biol. 2000, 151:277-288.
    • (2000) J.Cell Biol. , vol.151 , pp. 277-288
    • Kanaji, S.1    Iwahashi, J.2    Kida, Y.3    Sakaguchi, M.4    Mihara, K.5
  • 20
    • 1142274208 scopus 로고    scopus 로고
    • Cdh1-APC controls axonal growth and patterning in the mammalian brain
    • Konishi Y., Stegmüller J., Matsuda T., Bonni S., Bonni A. Cdh1-APC controls axonal growth and patterning in the mammalian brain. Science 2004, 303:1026-1030.
    • (2004) Science , vol.303 , pp. 1026-1030
    • Konishi, Y.1    Stegmüller, J.2    Matsuda, T.3    Bonni, S.4    Bonni, A.5
  • 21
    • 78049395303 scopus 로고    scopus 로고
    • Ubiquitination in postsynaptic function and plasticity
    • Mabb A.M., Ehlers M.D. Ubiquitination in postsynaptic function and plasticity. Annu. Rev. Cell Dev. Biol. 2010, 26:179-210.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 179-210
    • Mabb, A.M.1    Ehlers, M.D.2
  • 22
    • 33847727050 scopus 로고    scopus 로고
    • Ubiquitin proteasome system (UPS): what can chromatin do for you?
    • O'Connell B.C., Harper J.W. Ubiquitin proteasome system (UPS): what can chromatin do for you?. Curr. Opin. Cell Biol. 2007, 19:206-214.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 206-214
    • O'Connell, B.C.1    Harper, J.W.2
  • 24
    • 84155197392 scopus 로고    scopus 로고
    • A TRPC5-regulated calcium signaling pathway controls dendrite patterning in the mammalian brain
    • Puram S.V., Riccio A., Koirala S., Ikeuchi Y., Kim A.H., Corfas G., Bonni A. A TRPC5-regulated calcium signaling pathway controls dendrite patterning in the mammalian brain. Genes Dev. 2011, 25:2659-2673.
    • (2011) Genes Dev. , vol.25 , pp. 2659-2673
    • Puram, S.V.1    Riccio, A.2    Koirala, S.3    Ikeuchi, Y.4    Kim, A.H.5    Corfas, G.6    Bonni, A.7
  • 26
  • 27
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer T.P., Ahn S., Meyer T. Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr. Biol. 1998, 8:343-346.
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 29
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker S., Sadis S., Rubin D.M., Glickman M., Fu H., Coux O., Wefes I., Finley D., Vierstra R.D. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 1996, 16:6020-6028.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 30
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: functions, mysteries, uses
    • Varshavsky A. The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 1996, 93:12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 31
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R., Oania R., Graumann J., Deshaies R.J. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 2004, 118:99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 32
    • 84875853339 scopus 로고    scopus 로고
    • Spatial organization of ubiquitin ligase pathways orchestrates neuronal connectivity
    • Yamada T., Yang Y., Bonni A. Spatial organization of ubiquitin ligase pathways orchestrates neuronal connectivity. Trends Neurosci. 2013, 36:218-226.
    • (2013) Trends Neurosci. , vol.36 , pp. 218-226
    • Yamada, T.1    Yang, Y.2    Bonni, A.3
  • 33
    • 0032489524 scopus 로고    scopus 로고
    • Characterization of two polyubiquitin binding sites in the 26S protease subunit 5a
    • Young P., Deveraux Q., Beal R.E., Pickart C.M., Rechsteiner M. Characterization of two polyubiquitin binding sites in the 26S protease subunit 5a. J.Biol. Chem. 1998, 273:5461-5467.
    • (1998) J.Biol. Chem. , vol.273 , pp. 5461-5467
    • Young, P.1    Deveraux, Q.2    Beal, R.E.3    Pickart, C.M.4    Rechsteiner, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.