메뉴 건너뛰기




Volumn 15, Issue 22, 2005, Pages 2050-2055

Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; GAN PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; TUBULIN COFACTOR B, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 27844560722     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2005.10.052     Document Type: Article
Times cited : (75)

References (25)
  • 2
    • 0025018176 scopus 로고
    • Giant axonal neuropathy (GAN): An immunohistochemical and ultrastructural study report of a Latin American case
    • A.L. Taratuto, G. Sevlever, M. Saccoliti, L. Caceres, and M. Schultz Giant axonal neuropathy (GAN): An immunohistochemical and ultrastructural study report of a Latin American case Acta Neuropathol. (Berl.) 80 1990 680 683
    • (1990) Acta Neuropathol. (Berl.) , vol.80 , pp. 680-683
    • Taratuto, A.L.1    Sevlever, G.2    Saccoliti, M.3    Caceres, L.4    Schultz, M.5
  • 3
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • A. Ciechanover, and P. Brundin The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg Neuron 40 2003 427 446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 4
    • 0842346437 scopus 로고    scopus 로고
    • Principles of tumor suppression
    • C.J. Sherr Principles of tumor suppression Cell 116 2004 235 246
    • (2004) Cell , vol.116 , pp. 235-246
    • Sherr, C.J.1
  • 5
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • G. Tian, S.A. Lewis, B. Feierbach, T. Stearns, H. Rommelaere, C. Ampe, and N.J. Cowan Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors J. Cell Biol. 138 1997 821 832
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 7
  • 8
    • 0032706257 scopus 로고    scopus 로고
    • A chaperone with a hydrophilic surface
    • N.J. Cowan, and S.A. Lewis A chaperone with a hydrophilic surface Nat. Struct. Biol. 6 1999 990 991
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 990-991
    • Cowan, N.J.1    Lewis, S.A.2
  • 15
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • L. Xu, Y. Wei, J. Reboul, P. Vaglio, T.H. Shin, M. Vidal, S.J. Elledge, and J.W. Harper BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3 Nature 425 2003 316 321
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8
  • 16
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • M. Furukawa, Y.J. He, C. Borchers, and Y. Xiong Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases Nat. Cell Biol. 5 2003 1001 1007
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 17
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • R. Geyer, S. Wee, S. Anderson, J. Yates, and D.A. Wolf BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases Mol. Cell 12 2003 783 790
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 18
    • 1942434716 scopus 로고    scopus 로고
    • RhoBTB2 is a substrate of the mammalian Cul3 ubiquitin ligase complex
    • A. Wilkins, Q. Ping, and C.L. Carpenter RhoBTB2 is a substrate of the mammalian Cul3 ubiquitin ligase complex Genes Dev. 18 2004 856 861
    • (2004) Genes Dev. , vol.18 , pp. 856-861
    • Wilkins, A.1    Ping, Q.2    Carpenter, C.L.3
  • 19
    • 0032824097 scopus 로고    scopus 로고
    • Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast
    • P.A. Radcliffe, D. Hirata, L. Vardy, and T. Toda Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast Mol. Biol. Cell 10 1999 2987 3001
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2987-3001
    • Radcliffe, P.A.1    Hirata, D.2    Vardy, L.3    Toda, T.4
  • 23
    • 0037175395 scopus 로고    scopus 로고
    • Missense mutation in the tubulin-specific chaperone e (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease
    • H. Bommel, G. Xie, W. Rossoll, S. Wiese, S. Jablonka, T. Boehm, and M. Sendtner Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease J. Cell Biol. 159 2002 563 569
    • (2002) J. Cell Biol. , vol.159 , pp. 563-569
    • Bommel, H.1    Xie, G.2    Rossoll, W.3    Wiese, S.4    Jablonka, S.5    Boehm, T.6    Sendtner, M.7
  • 24
    • 0034729382 scopus 로고    scopus 로고
    • ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
    • A. Bhamidipati, S.A. Lewis, and N.J. Cowan ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin J. Cell Biol. 149 2000 1087 1096
    • (2000) J. Cell Biol. , vol.149 , pp. 1087-1096
    • Bhamidipati, A.1    Lewis, S.A.2    Cowan, N.J.3
  • 25
    • 0034678076 scopus 로고    scopus 로고
    • Tubulin folding cofactor D is a microtubule destabilizing protein
    • L. Martin, M.L. Fanarraga, K. Aloria, and J.C. Zabala Tubulin folding cofactor D is a microtubule destabilizing protein FEBS Lett. 470 2000 93 95
    • (2000) FEBS Lett. , vol.470 , pp. 93-95
    • Martin, L.1    Fanarraga, M.L.2    Aloria, K.3    Zabala, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.