메뉴 건너뛰기




Volumn 371, Issue 1, 2008, Pages 10-15

The alpha-5 helix of Bax is sensitive to ubiquitin-dependent degradation

Author keywords

Apoptosis; Bax; Degradation

Indexed keywords

MUTANT PROTEIN; PROTEASOME; PROTEIN BAX; PROTEIN BAX ALPHA5; UBIQUITIN;

EID: 42749083788     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.122     Document Type: Article
Times cited : (6)

References (22)
  • 1
    • 2342570286 scopus 로고    scopus 로고
    • Bax to Bcl-2 ratio and Ki-67 index are useful predictors of neoadjuvant chemoradiation therapy in bladder cancer
    • Matsumoto H., Wada T., Fukunaga K., Yoshihiro S., Matsuyama H., and Naito K. Bax to Bcl-2 ratio and Ki-67 index are useful predictors of neoadjuvant chemoradiation therapy in bladder cancer. Jpn. J. Clin. Oncol. 34 (2004) 124-130
    • (2004) Jpn. J. Clin. Oncol. , vol.34 , pp. 124-130
    • Matsumoto, H.1    Wada, T.2    Fukunaga, K.3    Yoshihiro, S.4    Matsuyama, H.5    Naito, K.6
  • 7
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression
    • Li B., and Dou Q.P. Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression. Proc. Natl. Acad. Sci. USA 97 (2000) 3850-3855
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 8
    • 41949136647 scopus 로고    scopus 로고
    • Bortezomib blocks Bax degradation in malignant B-cells during treatment with TRAIL
    • Liu F.T., Agrawal S.G., Gribben J.G., Ye H., Du M.Q., Newland A.C., and Jia L. Bortezomib blocks Bax degradation in malignant B-cells during treatment with TRAIL. Blood 111 (2008) 2797-2805
    • (2008) Blood , vol.111 , pp. 2797-2805
    • Liu, F.T.1    Agrawal, S.G.2    Gribben, J.G.3    Ye, H.4    Du, M.Q.5    Newland, A.C.6    Jia, L.7
  • 10
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., and Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103 (2000) 645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 11
    • 9744244990 scopus 로고    scopus 로고
    • The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA
    • Cartron P.F., Gallenne T., Bougras G., Gautier F., Manero F., Vusio P., Meflah K., Vallette F.M., and Juin P. The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA. Mol. Cell 16 (2004) 807-818
    • (2004) Mol. Cell , vol.16 , pp. 807-818
    • Cartron, P.F.1    Gallenne, T.2    Bougras, G.3    Gautier, F.4    Manero, F.5    Vusio, P.6    Meflah, K.7    Vallette, F.M.8    Juin, P.9
  • 12
    • 34250335634 scopus 로고    scopus 로고
    • The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL
    • Parikh N., Koshy C., Dhayabaran V., Perumalsamy L.R., Sowdhamini R., and Sarin A. The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL. BMC Cell Biol. 8 (2007) 16
    • (2007) BMC Cell Biol. , vol.8 , pp. 16
    • Parikh, N.1    Koshy, C.2    Dhayabaran, V.3    Perumalsamy, L.R.4    Sowdhamini, R.5    Sarin, A.6
  • 13
    • 34547629939 scopus 로고    scopus 로고
    • A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax
    • George N.M., Evans J.J., and Luo X. A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax. Genes Dev. 21 (2007) 1937-1948
    • (2007) Genes Dev. , vol.21 , pp. 1937-1948
    • George, N.M.1    Evans, J.J.2    Luo, X.3
  • 14
    • 0033956449 scopus 로고    scopus 로고
    • The putative pore-forming domain of Bax regulates mitochondrial localization and interaction with Bcl-X(L)
    • Nouraini S., Six E., Matsuyama S., Krajewski S., and Reed J.C. The putative pore-forming domain of Bax regulates mitochondrial localization and interaction with Bcl-X(L). Mol. Cell Biol. 20 (2000) 1604-1615
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1604-1615
    • Nouraini, S.1    Six, E.2    Matsuyama, S.3    Krajewski, S.4    Reed, J.C.5
  • 15
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M., Millar D.G., Yong V.W., Korsmeyer S.J., and Shore G.C. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268 (1993) 25265-25268
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Millar, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 18
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of Bid. A functional consequence on apoptosis induction
    • Breitschopf K., Zeiher A.M., and Dimmeler S. Ubiquitin-mediated degradation of the proapoptotic active form of Bid. A functional consequence on apoptosis induction. J. Biol. Chem. 275 (2000) 21648-21652
    • (2000) J. Biol. Chem. , vol.275 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 19
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti A.M., Treier M., and Bohmann D. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275 (1997) 400-402
    • (1997) Science , vol.275 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 20
    • 42749091648 scopus 로고    scopus 로고
    • H. Wolfgang, D.H. Wolf. Molecular Biology Intelligence Unite, 12, Proteasomes: The World of Regulatory Proteolysis. Eurekah.com/Landes Bioscience, Texas, USA, 2000.
    • H. Wolfgang, D.H. Wolf. Molecular Biology Intelligence Unite, 12, Proteasomes: The World of Regulatory Proteolysis. Eurekah.com/Landes Bioscience, Texas, USA, 2000.
  • 22
    • 0141481980 scopus 로고    scopus 로고
    • Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax
    • Cao X., Deng X., and May W.S. Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax. Blood 102 (2003) 2605-2614
    • (2003) Blood , vol.102 , pp. 2605-2614
    • Cao, X.1    Deng, X.2    May, W.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.