메뉴 건너뛰기




Volumn 33, Issue 5, 2013, Pages

Molecular interactions of Bcl-2 and Bcl-xL with mortalin: Identification and functional characterization

Author keywords

Bcl 2; Bcl xL; Interaction; Mortalin; P53 activation; Senescence

Indexed keywords

CHAPERONE; MORTALIN; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 84887037147     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20130034     Document Type: Article
Times cited : (22)

References (50)
  • 2
    • 33644928489 scopus 로고    scopus 로고
    • Bcl-2 family of apoptosis-related genes: Functions and clinical implications in cancer
    • Thomadaki, H. and Scorilas, A. (2006) Bcl-2 family of apoptosis-related genes: functions and clinical implications in cancer. Crit. Rev. Clin. Lab. Sci. 43, 1-67
    • (2006) Crit. Rev. Clin. Lab. Sci. , vol.43 , pp. 1-67
    • Thomadaki, H.1    Scorilas, A.2
  • 4
    • 0034722884 scopus 로고    scopus 로고
    • Bcl-2 family proteins as targets for anticancer drug design
    • Huang, Z. (2000) Bcl-2 family proteins as targets for anticancer drug design. Oncogene 19, 6627-6631
    • (2000) Oncogene , vol.19 , pp. 6627-6631
    • Huang, Z.1
  • 5
    • 0347089015 scopus 로고    scopus 로고
    • Mono- and multisite phosphorylation enhances Bcl-2's antiapoptotic function and inhibition of cell cycle entry functions
    • Deng, X., Gao, F., Flagg, T. and May, W. S. , Jr. (2004) Mono- and multisite phosphorylation enhances Bcl-2's antiapoptotic function and inhibition of cell cycle entry functions. Proc. Natl. Acad. Sci. USA 101, 153-158
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 153-158
    • Deng, X.1    Gao, F.2    Flagg, T.3    May Jr., W.S.4
  • 7
    • 14244268253 scopus 로고    scopus 로고
    • Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells
    • Liu, Y., Liu, W., Song, X. D. and Zuo, J. (2005) Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Mol. Cell. Biochem. 268, 45-51
    • (2005) Mol. Cell. Biochem. , vol.268 , pp. 45-51
    • Liu, Y.1    Liu, W.2    Song, X.D.3    Zuo, J.4
  • 8
    • 0034595925 scopus 로고    scopus 로고
    • Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2
    • Kaul, S. C., Reddel, R. R., Sugihara, T., Mitsui, Y. and Wadhwa, R. (2000) Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2. FEBS Lett. 474, 159-164
    • (2000) FEBS Lett. , vol.474 , pp. 159-164
    • Kaul, S.C.1    Reddel, R.R.2    Sugihara, T.3    Mitsui, Y.4    Wadhwa, R.5
  • 9
    • 0037447901 scopus 로고    scopus 로고
    • Overexpressed mortalin (mot-2)/mthsp70/GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts
    • Kaul, S. C., Yaguchi, T., Taira, K., Reddel, R. R. and Wadhwa, R. (2003) Overexpressed mortalin (mot-2)/mthsp70/GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts. Exp. Cell Res. 286, 96-101
    • (2003) Exp. Cell Res. , vol.286 , pp. 96-101
    • Kaul, S.C.1    Yaguchi, T.2    Taira, K.3    Reddel, R.R.4    Wadhwa, R.5
  • 10
    • 59149091608 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia
    • Xu, L., Voloboueva, L. A., Ouyang, Y., Emery, J. F. and Giffard, R. G. (2009) Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J Cereb Blood Flow Metab. 29, 365-74
    • (2009) J Cereb Blood Flow Metab. , vol.29 , pp. 365-74
    • Xu, L.1    Voloboueva, L.A.2    Ouyang, Y.3    Emery, J.F.4    Giffard, R.G.5
  • 13
    • 0037051942 scopus 로고    scopus 로고
    • Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75
    • Yokoyama, K., Fukumoto, K., Murakami, T., Harada, S., Hosono, R., Wadhwa, R., Mitsui, Y. and Ohkuma, S. (2002) Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75. FEBS Lett. 516, 53-57
    • (2002) FEBS Lett. , vol.516 , pp. 53-57
    • Yokoyama, K.1    Fukumoto, K.2    Murakami, T.3    Harada, S.4    Hosono, R.5    Wadhwa, R.6    Mitsui, Y.7    Ohkuma, S.8
  • 14
    • 0042091934 scopus 로고    scopus 로고
    • Targeting mortalin using conventional and RNA-helicase-coupled hammerhead ribozymes
    • Wadhwa, R., Ando, H., Kawasaki, H., Taira, K. and Kaul, S. C. (2003) Targeting mortalin using conventional and RNA-helicase-coupled hammerhead ribozymes. EMBO Rep. 4, 595-601
    • (2003) EMBO Rep. , vol.4 , pp. 595-601
    • Wadhwa, R.1    Ando, H.2    Kawasaki, H.3    Taira, K.4    Kaul, S.C.5
  • 15
    • 13644254746 scopus 로고    scopus 로고
    • Reduction in mortalin level by its antisense expression causes senescence-like growth arrest in human immortalized cells
    • Wadhwa, R., Takano, S., Taira, K. and Kaul, S. C. (2004) Reduction in mortalin level by its antisense expression causes senescence-like growth arrest in human immortalized cells. J. Gene Med. 6, 439-444
    • (2004) J. Gene Med. , vol.6 , pp. 439-444
    • Wadhwa, R.1    Takano, S.2    Taira, K.3    Kaul, S.C.4
  • 16
    • 34247171756 scopus 로고    scopus 로고
    • Knockdown of mitochondrial heat shock protein 70 promotes progeria-like phenotypes in Caenorhabditis elegans
    • Kimura, K., Tanaka, N., Nakamura, N., Takano, S. and Ohkuma, S. (2007) Knockdown of mitochondrial heat shock protein 70 promotes progeria-like phenotypes in Caenorhabditis elegans. J. Biol. Chem. 282, 5910-5918
    • (2007) J. Biol. Chem. , vol.282 , pp. 5910-5918
    • Kimura, K.1    Tanaka, N.2    Nakamura, N.3    Takano, S.4    Ohkuma, S.5
  • 18
    • 28244470279 scopus 로고    scopus 로고
    • Activation of wild type p53 function by its mortalin-binding, cytoplasmically localizing carboxyl terminus peptides
    • Kaul, S. C., Aida, S., Yaguchi, T., Kaur, K. and Wadhwa, R. (2005) Activation of wild type p53 function by its mortalin-binding, cytoplasmically localizing carboxyl terminus peptides. J. Biol. Chem. 280, 39373-39379
    • (2005) J. Biol. Chem. , vol.280 , pp. 39373-39379
    • Kaul, S.C.1    Aida, S.2    Yaguchi, T.3    Kaur, K.4    Wadhwa, R.5
  • 19
    • 33748286872 scopus 로고    scopus 로고
    • Mortalin controls centrosome duplication via modulating centrosomal localization of p53
    • Ma, Z., Izumi, H., Kanai, M., Kabuyama, Y., Ahn, N. G. and Fukasawa, K. (2006) Mortalin controls centrosome duplication via modulating centrosomal localization of p53. Oncogene 25, 5377-5390
    • (2006) Oncogene , vol.25 , pp. 5377-5390
    • Ma, Z.1    Izumi, H.2    Kanai, M.3    Kabuyama, Y.4    Ahn, N.G.5    Fukasawa, K.6
  • 20
    • 79955827220 scopus 로고    scopus 로고
    • Mortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy
    • Lu, W. J., Lee, N. P., Kaul, S. C., Lan, F., Poon, R. T., Wadhwa, R. and Luk, J. M. (2011) Mortalin-p53 interaction in cancer cells is stress dependent and constitutes a selective target for cancer therapy. Cell Death Differ. 18, 1046-1056
    • (2011) Cell Death Differ. , vol.18 , pp. 1046-1056
    • Lu, W.J.1    Lee, N.P.2    Kaul, S.C.3    Lan, F.4    Poon, R.T.5    Wadhwa, R.6    Luk, J.M.7
  • 21
    • 80052036411 scopus 로고    scopus 로고
    • Induction of mutant p53-dependent apoptosis in human hepatocellular carcinoma by targeting stress protein mortalin
    • Lu, W. J., Lee, N. P., Kaul, S. C., Lan, F., Poon, R. T. P., Wadhwa, R. and Luk, J. M. (2011) Induction of mutant p53-dependent apoptosis in human hepatocellular carcinoma by targeting stress protein mortalin. Int. J. Cancer 129, 1806-1814
    • (2011) Int. J. Cancer , vol.129 , pp. 1806-1814
    • Lu, W.J.1    Lee, N.P.2    Kaul, S.C.3    Lan, F.4    Poon, R.T.P.5    Wadhwa, R.6    Luk, J.M.7
  • 22
    • 0028543583 scopus 로고
    • Mitochondrial stress protein actions during chemically induced renal proximal tubule cell death
    • Bruschi, S. A. and Lindsay, J. G. (1994) Mitochondrial stress protein actions during chemically induced renal proximal tubule cell death. Biochem. Cell Biol. 72, 663-667
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 663-667
    • Bruschi, S.A.1    Lindsay, J.G.2
  • 23
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells
    • Qu, M., Zhou, Z., Xu, S., Chen, C., Yu, Z. and Wang, D. (2011) Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells. Brain Res. 1368, 336-345
    • (2011) Brain Res. , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5    Wang, D.6
  • 24
    • 2142853088 scopus 로고    scopus 로고
    • Detection of mitochondrial localization of p53
    • Mihara, M. and Moll, U. M. (2003) Detection of mitochondrial localization of p53. Methods Mol. Biol. 234, 203-209
    • (2003) Methods Mol. Biol. , vol.234 , pp. 203-209
    • Mihara, M.1    Moll, U.M.2
  • 25
    • 33745017872 scopus 로고    scopus 로고
    • Bcl2's flexible loop domain regulates p53 binding and survival
    • Deng, X., Gao, F., Flagg, T., Anderson, J. and May, W. S. (2006) Bcl2's flexible loop domain regulates p53 binding and survival. Mol. Cell Biol. 26, 4421-4434
    • (2006) Mol. Cell Biol. , vol.26 , pp. 4421-4434
    • Deng, X.1    Gao, F.2    Flagg, T.3    Anderson, J.4    May, W.S.5
  • 26
    • 0442323478 scopus 로고    scopus 로고
    • Defining the p53 DNA-binding domain/Bcl-xL-binding interface using NMR
    • Petros, A. M., Gunasekera, A., Xu, N., Olejniczak, E. T. and Fesik, S. W. (2004) Defining the p53 DNA-binding domain/Bcl-xL-binding interface using NMR. FEBS Lett. 559, 171-174
    • (2004) FEBS Lett. , vol.559 , pp. 171-174
    • Petros, A.M.1    Gunasekera, A.2    Xu, N.3    Olejniczak, E.T.4    Fesik, S.W.5
  • 27
    • 2342431845 scopus 로고    scopus 로고
    • Bcl-xL and E1B-19K proteins inhibit p53-induced irreversible growth arrest and senescence by preventing reactive oxygen species-dependent p38 activation
    • Jung, M. S., Jin, D. H., Chae, H. D., Kang, S., Kim, S. C., Bang, Y. J., Choi, T. S., Choi, K. S. and Shin, D. Y. (2004) Bcl-xL and E1B-19K proteins inhibit p53-induced irreversible growth arrest and senescence by preventing reactive oxygen species-dependent p38 activation. J. Biol. Chem. 279, 17765-17771
    • (2004) J. Biol. Chem. , vol.279 , pp. 17765-17771
    • Jung, M.S.1    Jin, D.H.2    Chae, H.D.3    Kang, S.4    Kim, S.C.5    Bang, Y.J.6    Choi, T.S.7    Choi, K.S.8    Shin, D.Y.9
  • 28
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A. and Sali, A. (2003) Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol. 374, 461-491
    • (2003) Methods Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 29
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R. and Bonvin, A. M. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 30
    • 36949010567 scopus 로고    scopus 로고
    • InterProSurf: A web server for predicting interacting sites on protein surfaces
    • Negi, S. S., Schein, C. H., Oezguen, N., Power, T. D. and Braun, W. (2007) InterProSurf: a web server for predicting interacting sites on protein surfaces. Bioinformatics 23, 3397-3399
    • (2007) Bioinformatics , vol.23 , pp. 3397-3399
    • Negi, S.S.1    Schein, C.H.2    Oezguen, N.3    Power, T.D.4    Braun, W.5
  • 31
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • Reynolds, C., Damerell, D. and Jones, S. (2009) ProtorP: a protein-protein interaction analysis server. Bioinformatics 25, 413-414
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 32
    • 77954057644 scopus 로고    scopus 로고
    • Version 2.4, D.E. Shaw Research, New York, NY, 2010. Maestro-Desmond Interoperability Tools, Version 2.4, Schrödinger, New York, NY
    • Desmond Molecular Dynamics System (2010) Version 2.4, D.E. Shaw Research, New York, NY, 2010. Maestro-Desmond Interoperability Tools, Version 2.4, Schrödinger, New York, NY
    • (2010) Desmond Molecular Dynamics System
  • 34
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger, S., Germeroth, L., Schneider-Mergener, J. and Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 35
    • 33646496005 scopus 로고    scopus 로고
    • Mortalin-based cytoplasmic sequestration of p53 in a nonmammalian cancer model
    • Walker, C., Bottger, S. and Low, B. (2006) Mortalin-based cytoplasmic sequestration of p53 in a nonmammalian cancer model. Am. J. Pathol. 168, 1526-1530
    • (2006) Am. J. Pathol. , vol.168 , pp. 1526-1530
    • Walker, C.1    Bottger, S.2    Low, B.3
  • 36
    • 0036346345 scopus 로고    scopus 로고
    • Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein
    • Wadhwa, R., Yaguchi, T., Hasan, M. K., Mitsui, Y., Reddel, R. R. and Kaul, S. C. (2002) Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein. Exp. Cell Res. 274, 246-253
    • (2002) Exp. Cell Res. , vol.274 , pp. 246-253
    • Wadhwa, R.1    Yaguchi, T.2    Hasan, M.K.3    Mitsui, Y.4    Reddel, R.R.5    Kaul, S.C.6
  • 37
    • 0345654336 scopus 로고    scopus 로고
    • Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes
    • Bertram, M. J., Berube, N. G., Hang-Swanson, X., Ran, Q., Leung, J. K., Bryce, S., Spurgers, K., Bick, R. J., Baldini, A., Ning, Y. et al. (1999) Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes. Mol. Cell Biol. 19, 1479-1485
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1479-1485
    • Bertram, M.J.1    Berube, N.G.2    Hang-Swanson, X.3    Ran, Q.4    Leung, J.K.5    Bryce, S.6    Spurgers, K.7    Bick, R.J.8    Baldini, A.9    Et Al., N.Y.10
  • 38
    • 0031572306 scopus 로고    scopus 로고
    • Decrease in amplified telomeric sequences and induction of senescence markers by introduction of human chromosome 7 or its segments in SUSM-1
    • Nakabayashi, K., Ogata, T., Fujii, M., Tahara, H., Ide, T., Wadhwa, R., Kaul, S. C., Mitsui, Y. and Ayusawa, D. (1997) Decrease in amplified telomeric sequences and induction of senescence markers by introduction of human chromosome 7 or its segments in SUSM-1. Exp. Cell Res. 235, 345-353
    • (1997) Exp. Cell Res. , vol.235 , pp. 345-353
    • Nakabayashi, K.1    Ogata, T.2    Fujii, M.3    Tahara, H.4    Ide, T.5    Wadhwa, R.6    Kaul, S.C.7    Mitsui, Y.8    Ayusawa, D.9
  • 39
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • Wadhwa, R., Sugihara, T., Yoshida, A., Nomura, H., Reddel, R. R., Simpson, R., Maruta, H. and Kaul, S. C. (2000) Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res. 60, 6818-6821
    • (2000) Cancer Res. , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 41
    • 34247536630 scopus 로고    scopus 로고
    • Selective killing of cancer cells by leaf extract of Ashwagandha: Identification of a tumor-inhibitory factor and the first molecular insights to its effect
    • Widodo, N., Kaur, K., Shrestha, B. G., Takagi, Y., Ishii, T., Wadhwa, R. and Kaul, S. C. (2007) Selective killing of cancer cells by leaf extract of Ashwagandha: identification of a tumor-inhibitory factor and the first molecular insights to its effect. Clin. Cancer Res 13, 2298-2306
    • (2007) Clin. Cancer Res , vol.13 , pp. 2298-2306
    • Widodo, N.1    Kaur, K.2    Shrestha, B.G.3    Takagi, Y.4    Ishii, T.5    Wadhwa, R.6    Kaul, S.C.7
  • 43
    • 20544437817 scopus 로고    scopus 로고
    • Unknotting the roles of Bcl-2 and Bcl-xL in cell death
    • Kim, R. (2005) Unknotting the roles of Bcl-2 and Bcl-xL in cell death. Biochem. Biophys. Res. Commun. 333, 336-343
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 336-343
    • Kim, R.1
  • 47
    • 0037403345 scopus 로고    scopus 로고
    • Life span shortening of normal fibroblasts by overexpression of BCL-2: A result of potent increase in cell death
    • Kumazaki, T., Sasaki, M., Nishiyama, M., Teranishi, Y., Sumida, H., Eboshima, A. and Mitsui, Y. (2003) Life span shortening of normal fibroblasts by overexpression of BCL-2: a result of potent increase in cell death. Exp. Cell Res. 285, 299-308
    • (2003) Exp. Cell Res. , vol.285 , pp. 299-308
    • Kumazaki, T.1    Sasaki, M.2    Nishiyama, M.3    Teranishi, Y.4    Sumida, H.5    Eboshima, A.6    Mitsui, Y.7
  • 48
    • 15844397398 scopus 로고    scopus 로고
    • Diminished cell proliferation associated with the death protective activity of Bcl-2
    • Borner, C. (1996) Diminished cell proliferation associated with the death protective activity of Bcl-2. J. Biol. Chem. 271, 12695-12698
    • (1996) J. Biol. Chem. , vol.271 , pp. 12695-12698
    • Borner, C.1
  • 49
    • 0029938724 scopus 로고    scopus 로고
    • Regulation of cell division cycle progression by Bcl-2 expression: A potential mechanism for inhibition of programmed cell death
    • Mazel, S., Burtrum, D. and Petrie, H. T. (1996) Regulation of cell division cycle progression by Bcl-2 expression: a potential mechanism for inhibition of programmed cell death. J. Exp. Med. 183, 2219-2226
    • (1996) J. Exp. Med. , vol.183 , pp. 2219-2226
    • Mazel, S.1    Burtrum, D.2    Petrie, H.T.3
  • 50
    • 0029805403 scopus 로고    scopus 로고
    • Bcl-2 has a cell cycle inhibitory function separable from its enhancement of cell survival
    • Vairo, G., Innes, K. M. and Adams, J. M. (1996) Bcl-2 has a cell cycle inhibitory function separable from its enhancement of cell survival. Oncogene 13, 1511-1519
    • (1996) Oncogene , vol.13 , pp. 1511-1519
    • Vairo, G.1    Innes, K.M.2    Adams, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.