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Volumn 30, Issue 10, 2016, Pages 1240-1250

Physiological restraint of Bak by Bcl-xL is essential for cell survival

Author keywords

Apoptosis; Bak; Bcl 2; Bcl xL; BH3

Indexed keywords

GLYCINE; LEUCINE; PROTEIN BAK; PROTEIN BCL XL; ANTINEOPLASTIC AGENT; PROTEIN BCL X; PROTEIN BINDING;

EID: 84969900687     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.279414.116     Document Type: Article
Times cited : (41)

References (43)
  • 1
    • 57549090198 scopus 로고    scopus 로고
    • NF-κB1 and c-Rel cooperate to promote the survival of TLR4-activated B cells by neutralizing Bim via distinct mechanisms
    • Banerjee A, Grumont R, Gugasyan R, White C, Strasser A, Gerondakis S. 2008. NF-κB1 and c-Rel cooperate to promote the survival of TLR4-activated B cells by neutralizing Bim via distinct mechanisms. Blood 112: 5063-5073.
    • (2008) Blood , vol.112 , pp. 5063-5073
    • Banerjee, A.1    Grumont, R.2    Gugasyan, R.3    White, C.4    Strasser, A.5    Gerondakis, S.6
  • 2
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet P, Metcalf D, Huang DC, Tarlinton DM, Kay TW, Kontgen F, Adams JM, Strasser A. 1999. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 286: 1735-1738.
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.3    Tarlinton, D.M.4    Kay, T.W.5    Kontgen, F.6    Adams, J.M.7    Strasser, A.8
  • 6
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-XL sequester BH3 domainonly molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, Korsmeyer SJ. 2001. BCL-2, BCL-XL sequester BH3 domainonly molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 8: 705-711.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 9
    • 84944729445 scopus 로고    scopus 로고
    • Constitutive BAK activation as a determinant of drug sensitivity in malignant lymphohematopoietic cells
    • Dai H, Ding H, Meng XW, Peterson KL, Schneider PA, Karp JE, Kaufmann SH. 2015. Constitutive BAK activation as a determinant of drug sensitivity in malignant lymphohematopoietic cells. Genes Dev 29: 2140-2152.
    • (2015) Genes Dev , vol.29 , pp. 2140-2152
    • Dai, H.1    Ding, H.2    Meng, X.W.3    Peterson, K.L.4    Schneider, P.A.5    Karp, J.E.6    Kaufmann, S.H.7
  • 11
  • 12
    • 0242653642 scopus 로고    scopus 로고
    • A family of leukemia inhibitory factor-binding peptides that can act as antagonists when conjugated to poly(Ethylene glycol)
    • Fairlie WD, Uboldi AD, Hemmings GJ, Smith BJ, Martin HM, Morgan PO, Baca M. 2003. A family of leukemia inhibitory factor-binding peptides that can act as antagonists when conjugated to poly(ethylene glycol). Biochemistry 42: 13193-13201.
    • (2003) Biochemistry , vol.42 , pp. 13193-13201
    • Fairlie, W.D.1    Uboldi, A.D.2    Hemmings, G.J.3    Smith, B.J.4    Martin, H.M.5    Morgan, P.O.6    Baca, M.7
  • 20
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T, Bouchier-Hayes L, Chipuk JE, Bonzon C, Sullivan BA, Green DR, Newmeyer DD. 2005. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 17: 525-535.
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 22
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • Leber B, Lin J, Andrews DW. 2010. Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene 29: 5221-5230.
    • (2010) Oncogene , vol.29 , pp. 5221-5230
    • Leber, B.1    Lin, J.2    Rews, D.W.3
  • 23
    • 34548047900 scopus 로고    scopus 로고
    • Crystal structure of ABT-737 complexed with Bcl-xL: Implications for selectivity of antagonists of the Bcl-2 family
    • Lee EF, Czabotar PE, Smith BJ, Deshayes K, Zobel K, Colman PM, Fairlie WD. 2007. Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family. Cell Death Differ 14: 1711-1713.
    • (2007) Cell Death Differ , vol.14 , pp. 1711-1713
    • Lee, E.F.1    Czabotar, P.E.2    Smith, B.J.3    Deshayes, K.4    Zobel, K.5    Colman, P.M.6    Fairlie, W.D.7
  • 26
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, Korsmeyer SJ. 2002. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 33
    • 33751544565 scopus 로고    scopus 로고
    • The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
    • Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K. 2006. The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 24: 677-688.
    • (2006) Mol Cell , vol.24 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.4    Shore, G.5    Gehring, K.6
  • 35
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • Oberstein A, Jeffrey PD, Shi Y. 2007. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 282: 13123-13132.
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 12544251669 scopus 로고    scopus 로고
    • Mitochondrial release of pro-apoptotic proteins: Electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes
    • Uren RT, Dewson G, Bonzon C, Lithgow T, Newmeyer DD, Kluck RM. 2005. Mitochondrial release of pro-apoptotic proteins: electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes. J Biol Chem 280: 2266-2274.
    • (2005) J Biol Chem , vol.280 , pp. 2266-2274
    • Uren, R.T.1    Dewson, G.2    Bonzon, C.3    Lithgow, T.4    Newmeyer, D.D.5    Kluck, R.M.6
  • 39
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl- 1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis SN, Chen L, Dewson G, Wei A, Naik E, Fletcher JI, Adams JM, Huang DC. 2005. Proapoptotic Bak is sequestered by Mcl- 1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19: 1294-1305.
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 41
    • 78649630259 scopus 로고    scopus 로고
    • Navitoclax, a targeted high-affinity inhibitor of BCL-2, in lymphoid malignancies: A phase 1 dose-escalation study of safety, pharmacokinetics, pharmacodynamics, and antitumour activity
    • Wilson WH, O’Connor OA, Czuczman MS, LaCasce AS, Gerecitano JF, Leonard JP, Tulpule A, Dunleavy K, Xiong H, Chiu YL, et al. 2010. Navitoclax, a targeted high-affinity inhibitor of BCL-2, in lymphoid malignancies: a phase 1 dose-escalation study of safety, pharmacokinetics, pharmacodynamics, and antitumour activity. Lancet Oncol 11: 1149-1159.
    • (2010) Lancet Oncol , vol.11 , pp. 1149-1159
    • Wilson, W.H.1    O’Connor, O.A.2    Czuczman, M.S.3    Lacasce, A.S.4    Gerecitano, J.F.5    Leonard, J.P.6    Tulpule, A.7    Dunleavy, K.8    Xiong, H.9    Chiu, Y.L.10
  • 42
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. 2008. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.