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Volumn 117, Issue 3, 2007, Pages 693-702

High-mobility group A1 inhibits p53 by cytoplasmic relocalization of its proapoptotic activator HIPK2

Author keywords

[No Author keywords available]

Indexed keywords

HIGH MOBILITY GROUP A PROTEIN; HOMEODOMAIN INTERACTING PROTEIN KINASE 2; PROTEIN P53;

EID: 33847398755     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI29852     Document Type: Article
Times cited : (84)

References (50)
  • 1
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., Giese, K., and Pagel, J. 1994. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10:94-100.
    • (1994) Trends Genet , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 2
    • 0025196283 scopus 로고
    • The A-T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure
    • Reeves, R., and Nissen, M.S. 1990. The A-T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure. J. Biol. Chem. 265:8573-8582.
    • (1990) J. Biol. Chem , vol.265 , pp. 8573-8582
    • Reeves, R.1    Nissen, M.S.2
  • 3
    • 0033664720 scopus 로고    scopus 로고
    • Structure and function of the HMGI(Y) family of architectural transcription factors
    • Reeves, R. 2000. Structure and function of the HMGI(Y) family of architectural transcription factors. Environ. Health Perspect. 108:803-809.
    • (2000) Environ. Health Perspect , vol.108 , pp. 803-809
    • Reeves, R.1
  • 4
    • 0029617947 scopus 로고
    • Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome
    • Thanos, D., and Maniatis, T. 1995. Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome. Cell. 83:1091-1100.
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 5
    • 0029094755 scopus 로고
    • Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C
    • Zhou, X., Benson, K.F., Ashar, H.R., and Chada, K. 1995. Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C. Nature. 376:771-774.
    • (1995) Nature , vol.376 , pp. 771-774
    • Zhou, X.1    Benson, K.F.2    Ashar, H.R.3    Chada, K.4
  • 6
    • 8044225313 scopus 로고    scopus 로고
    • High level expression of the HMGA1 gene during embryonic development
    • Chiappetta, G., et al. 1996. High level expression of the HMGA1 gene during embryonic development. Oncogene. 13:2439-2446.
    • (1996) Oncogene , vol.13 , pp. 2439-2446
    • Chiappetta, G.1
  • 7
    • 0028970056 scopus 로고
    • The expression of the high mobility group HMGA1 proteins correlates with the malignant phenotype of human thyroid neoplasms
    • Chiappetta, G., et al. 1995. The expression of the high mobility group HMGA1 proteins correlates with the malignant phenotype of human thyroid neoplasms. Oncogene. 10:1307-1314.
    • (1995) Oncogene , vol.10 , pp. 1307-1314
    • Chiappetta, G.1
  • 8
    • 0032530892 scopus 로고    scopus 로고
    • Detection of high mobility group I HMGI(Y) protein in the diagnosis of thyroid tumors: HMGI(Y) expression represents a potential diagnostic indicator of carcinoma
    • Chiappetta, G., et al. 1998. Detection of high mobility group I HMGI(Y) protein in the diagnosis of thyroid tumors: HMGI(Y) expression represents a potential diagnostic indicator of carcinoma. Cancer Res. 58:4193-4198.
    • (1998) Cancer Res , vol.58 , pp. 4193-4198
    • Chiappetta, G.1
  • 9
    • 9244229589 scopus 로고    scopus 로고
    • Human colorectal carcinomas express high levels of high mobility group HMGI(Y) proteins
    • Fedele, M., et al. 1996. Human colorectal carcinomas express high levels of high mobility group HMGI(Y) proteins. Cancer Res. 56:1896-1901.
    • (1996) Cancer Res , vol.56 , pp. 1896-1901
    • Fedele, M.1
  • 10
    • 0033559196 scopus 로고    scopus 로고
    • Determination of high mobility group I(Y) expression level in colorectal neoplasias: A potential diagnostic marker
    • Abe, N., et al. 1999. Determination of high mobility group I(Y) expression level in colorectal neoplasias: a potential diagnostic marker. Cancer Res. 59:1169-1174.
    • (1999) Cancer Res , vol.59 , pp. 1169-1174
    • Abe, N.1
  • 11
    • 0035863368 scopus 로고    scopus 로고
    • High mobility group HMGI(Y) protein expression in human colorectal hyperplastic and neoplastic diseases
    • Chiappetta, G., et al. 2001. High mobility group HMGI(Y) protein expression in human colorectal hyperplastic and neoplastic diseases. Int. J. Cancer. 91:147-151.
    • (2001) Int. J. Cancer , vol.91 , pp. 147-151
    • Chiappetta, G.1
  • 12
    • 0027441104 scopus 로고
    • Increased expression of high mobility group protein I(Y) in high grade prostatic cancer determined by in situ hybridization
    • Tamimi, Y., et al. 1993. Increased expression of high mobility group protein I(Y) in high grade prostatic cancer determined by in situ hybridization. Cancer Res. 53:5512-5516.
    • (1993) Cancer Res , vol.53 , pp. 5512-5516
    • Tamimi, Y.1
  • 13
    • 0036312129 scopus 로고    scopus 로고
    • Diagnostic significance of high mobility group I(Y) protein expression in intraductal papillary mucinous tumors of the pancreas
    • Abe, N., et al. 2002. Diagnostic significance of high mobility group I(Y) protein expression in intraductal papillary mucinous tumors of the pancreas. Pancreas. 25:198-204.
    • (2002) Pancreas , vol.25 , pp. 198-204
    • Abe, N.1
  • 14
    • 0032005220 scopus 로고    scopus 로고
    • Expression of HMGI(Y) proteins in squamous intraepithelial and invasive lesions of the uterine cervix
    • Bandiera, A., et al. 1998. Expression of HMGI(Y) proteins in squamous intraepithelial and invasive lesions of the uterine cervix. Cancer Res. 58:426-431.
    • (1998) Cancer Res , vol.58 , pp. 426-431
    • Bandiera, A.1
  • 15
    • 0041668179 scopus 로고    scopus 로고
    • HMGA1 protein overexpression is a frequent feature of epithelial ovarian carcinomas
    • Masciullo, V., et al. 2003. HMGA1 protein overexpression is a frequent feature of epithelial ovarian carcinomas. Carcinogenesis. 24:1191-1198.
    • (2003) Carcinogenesis , vol.24 , pp. 1191-1198
    • Masciullo, V.1
  • 16
    • 9344230370 scopus 로고    scopus 로고
    • HMGA1 protein overexpression in human breast carcinomas: Correlation with ErbB2 expression
    • Chiappetta, G., et al. 2004. HMGA1 protein overexpression in human breast carcinomas: correlation with ErbB2 expression. Clin. Cancer Res. 10:7637-7644.
    • (2004) Clin. Cancer Res , vol.10 , pp. 7637-7644
    • Chiappetta, G.1
  • 17
    • 0028860339 scopus 로고
    • Inhibition of HMGI-C protein synthesis suppresses retrovirally induced neoplastic transformation of rat thyroid cells
    • Berlingieri, M.T., et al. 1995. Inhibition of HMGI-C protein synthesis suppresses retrovirally induced neoplastic transformation of rat thyroid cells. Mol. Cell. Biol. 15:1545-1553.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 1545-1553
    • Berlingieri, M.T.1
  • 18
    • 85047699472 scopus 로고    scopus 로고
    • Thyroid cell transformation requires the expression of the HMGA1 proteins
    • Berlingieri, M.T., Pierantoni, G.M., Giancotti, V., Santoro, M., and Fusco, A. 2002. Thyroid cell transformation requires the expression of the HMGA1 proteins. Oncogene. 21:2971-2980.
    • (2002) Oncogene , vol.21 , pp. 2971-2980
    • Berlingieri, M.T.1    Pierantoni, G.M.2    Giancotti, V.3    Santoro, M.4    Fusco, A.5
  • 19
    • 0034636039 scopus 로고    scopus 로고
    • Adenovirus-mediated suppression of HMGI(Y) protein synthesis as potential therapy of human malignant neoplasias
    • Scala, S., Portella, G., Fedele, M., Chiappetta, G., and Fusco, A. 2000. Adenovirus-mediated suppression of HMGI(Y) protein synthesis as potential therapy of human malignant neoplasias. Proc. Natl. Acad. Sci. U. S. A. 97:4256-4261.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 4256-4261
    • Scala, S.1    Portella, G.2    Fedele, M.3    Chiappetta, G.4    Fusco, A.5
  • 20
    • 33747057745 scopus 로고    scopus 로고
    • High Mobility Group A1 (HMGA1) proteins interact with p53 and interfere with its apoptotic function
    • Pierantoni, G.M., et al. 2006. High Mobility Group A1 (HMGA1) proteins interact with p53 and interfere with its apoptotic function. Cell Death Differ. 13:1554-1563.
    • (2006) Cell Death Differ , vol.13 , pp. 1554-1563
    • Pierantoni, G.M.1
  • 21
    • 0034703742 scopus 로고    scopus 로고
    • p53: death star
    • Vousden, K.H. 2000. p53: death star. Cell. 103:691-694.
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1
  • 22
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B., Lane, D., and Levine, A.J. 2000. Surfing the p53 network. Nature. 408:307-310.
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 23
    • 0036527761 scopus 로고    scopus 로고
    • Dissecting p53 tumor suppressor functions in vivo
    • Schmitt, C.A., et al. 2002. Dissecting p53 tumor suppressor functions in vivo. Cancer Cell. 1:289-296.
    • (2002) Cancer Cell , vol.1 , pp. 289-296
    • Schmitt, C.A.1
  • 24
    • 0034031250 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the post-translational modification code
    • Appella, E., and Anderson, C.W. 2000. Signaling to p53: breaking the post-translational modification code. Pathol. Biol. 48:227-245.
    • (2000) Pathol. Biol , vol.48 , pp. 227-245
    • Appella, E.1    Anderson, C.W.2
  • 25
    • 3242883729 scopus 로고    scopus 로고
    • The p53 response to DNA damage
    • Meek, J. 2004. The p53 response to DNA damage. DNA Repair. 3:1049-1056.
    • (2004) DNA Repair , vol.3 , pp. 1049-1056
    • Meek, J.1
  • 26
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin, D.V., et al. 1999. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J. 18:6845-6854.
    • (1999) EMBO J , vol.18 , pp. 6845-6854
    • Bulavin, D.V.1
  • 27
    • 0034664733 scopus 로고    scopus 로고
    • p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53
    • Oda, K., et al. 2000. p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53. Cell. 102:849-862.
    • (2000) Cell , vol.102 , pp. 849-862
    • Oda, K.1
  • 28
    • 22544433198 scopus 로고    scopus 로고
    • Phosphorylation of human p53 at serine 46 determines promoter selection and whether apoptosis is attenuated or amplified
    • Mayo, L.D., et al. 2005. Phosphorylation of human p53 at serine 46 determines promoter selection and whether apoptosis is attenuated or amplified. J. Biol. Chem. 280:25953-25959.
    • (2005) J. Biol. Chem , vol.280 , pp. 25953-25959
    • Mayo, L.D.1
  • 29
    • 18244379872 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis
    • D'Orazi, G., et al. 2002. Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nat. Cell Biol. 4:11-19.
    • (2002) Nat. Cell Biol , vol.4 , pp. 11-19
    • D'Orazi, G.1
  • 30
    • 0036141392 scopus 로고    scopus 로고
    • Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2
    • Hofmann, T.G., et al. 2002. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nat. Cell Biol. 4:1-10.
    • (2002) Nat. Cell Biol , vol.4 , pp. 1-10
    • Hofmann, T.G.1
  • 31
    • 0037200042 scopus 로고    scopus 로고
    • Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo
    • Kim, E.-J., Park, J.-S., and Um, S.-J. 2002. Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo. J. Biol. Chem. 277:32020-32028.
    • (2002) J. Biol. Chem , vol.277 , pp. 32020-32028
    • Kim, E.-J.1    Park, J.-S.2    Um, S.-J.3
  • 32
    • 0142258245 scopus 로고    scopus 로고
    • Homeodomain interacting protein kinase 2 promotes apoptosis by down-regulating the transcriptional co-repressor CtBP
    • Zhang, Q., Yoshimatsu, Y., Hildebrand, J., Frisch, S.M., and Goodman, R.H. 2003. Homeodomain interacting protein kinase 2 promotes apoptosis by down-regulating the transcriptional co-repressor CtBP. Cell. 115:177-186.
    • (2003) Cell , vol.115 , pp. 177-186
    • Zhang, Q.1    Yoshimatsu, Y.2    Hildebrand, J.3    Frisch, S.M.4    Goodman, R.H.5
  • 33
    • 2542500783 scopus 로고    scopus 로고
    • HIPK2 overexpression leads to stabilization of p53 protein and increased p53 transcriptional activity by decreasing Mdm2 protein levels
    • Wang, Y., Debatin, K.M., and Hug, H. 2001. HIPK2 overexpression leads to stabilization of p53 protein and increased p53 transcriptional activity by decreasing Mdm2 protein levels. BMC Mol. Biol. 2:8-16.
    • (2001) BMC Mol. Biol , vol.2 , pp. 8-16
    • Wang, Y.1    Debatin, K.M.2    Hug, H.3
  • 34
    • 10644290911 scopus 로고    scopus 로고
    • Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation
    • Rui, Y., et al. 2004. Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation. EMBO J. 23:4583-4594.
    • (2004) EMBO J , vol.23 , pp. 4583-4594
    • Rui, Y.1
  • 35
    • 0035959740 scopus 로고    scopus 로고
    • High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth
    • Pierantoni, G.M., et al. 2001. High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth. Oncogene. 20:6132-6141.
    • (2001) Oncogene , vol.20 , pp. 6132-6141
    • Pierantoni, G.M.1
  • 36
    • 0345830383 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinase-2 activity and p53 phosphorylation are critical events for cisplatin-mediated apoptosis
    • Di Stefano, V., Rinaldo, C., Sacchi, A., Soddu, S., and D'Orazi, G. 2004. Homeodomain-interacting protein kinase-2 activity and p53 phosphorylation are critical events for cisplatin-mediated apoptosis. Exp. Cell Res. 293:311-320.
    • (2004) Exp. Cell Res , vol.293 , pp. 311-320
    • Di Stefano, V.1    Rinaldo, C.2    Sacchi, A.3    Soddu, S.4    D'Orazi, G.5
  • 37
    • 24644494726 scopus 로고    scopus 로고
    • HIPK2 contributes to PCAF-mediated p53 acetylation and selective transactivation of p21(Waf1) after nonapoptotic DNA damage
    • Di Stefano, V., Soddu, S., Sacchi, A., and D'Orazi, G. 2005. HIPK2 contributes to PCAF-mediated p53 acetylation and selective transactivation of p21(Waf1) after nonapoptotic DNA damage. Oncogene. 24:5431-5442.
    • (2005) Oncogene , vol.24 , pp. 5431-5442
    • Di Stefano, V.1    Soddu, S.2    Sacchi, A.3    D'Orazi, G.4
  • 38
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., et al. 1997. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature. 390:308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1
  • 39
    • 2442678753 scopus 로고    scopus 로고
    • PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains
    • Moller, A., et al. 2003. PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. Cancer Res. 63:4310-4314.
    • (2003) Cancer Res , vol.63 , pp. 4310-4314
    • Moller, A.1
  • 40
    • 33846616412 scopus 로고    scopus 로고
    • Bio-pathologic characteristics according to chromosome 11 aneusomy and cyclin D1 gene status in surgically resected stage I and II breast cancer: Identification of an adverse prognostic profile
    • In press
    • Mottolese, M., et al. 2007. Bio-pathologic characteristics according to chromosome 11 aneusomy and cyclin D1 gene status in surgically resected stage I and II breast cancer: identification of an adverse prognostic profile. Am. J. Surg. Pathol. In press.
    • (2007) Am. J. Surg. Pathol
    • Mottolese, M.1
  • 41
    • 33645515483 scopus 로고    scopus 로고
    • HMGA1 inhibits the function of p53 family members in thyroid cancer cells
    • Frasca, F., et al. 2006. HMGA1 inhibits the function of p53 family members in thyroid cancer cells. Cancer Res. 66:2980-2989.
    • (2006) Cancer Res , vol.66 , pp. 2980-2989
    • Frasca, F.1
  • 42
    • 33749641724 scopus 로고    scopus 로고
    • Ser58 of mouse p53 is the homologue of human Ser46 and is phosphorylated by HIPK2 in apoptosis
    • Cecchinelli, B., et al. 2006. Ser58 of mouse p53 is the homologue of human Ser46 and is phosphorylated by HIPK2 in apoptosis. Cell Death Differ. 13:1994-1997.
    • (2006) Cell Death Differ , vol.13 , pp. 1994-1997
    • Cecchinelli, B.1
  • 43
    • 33745020886 scopus 로고    scopus 로고
    • Repression of the antiapoptotic molecule galectin-3 by HIPK2-activated p53 is required for p53-induced apoptosis
    • Cecchinelli, B., et al. 2006. Repression of the antiapoptotic molecule galectin-3 by HIPK2-activated p53 is required for p53-induced apoptosis. Mol. Cell. Biol. 26:4746-4757.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 4746-4757
    • Cecchinelli, B.1
  • 44
    • 0038022702 scopus 로고    scopus 로고
    • Regulation of p53 functions: Let's meet at the nuclear bodies
    • Gostissa, M., Hofmann, T.G., Will, H., and Del Sal, G. 2003. Regulation of p53 functions: let's meet at the nuclear bodies. Curr. Opin. Cell Biol. 15:351-357.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 351-357
    • Gostissa, M.1    Hofmann, T.G.2    Will, H.3    Del Sal, G.4
  • 45
    • 0030448760 scopus 로고    scopus 로고
    • Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide
    • Ostermeyer, A.G., Runko, E., Winkfield, B., Ahn, B., and Moll, U.M. 1996. Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide. Proc. Natl. Acad. Sci. U. S. A. 93:15190-15194.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 15190-15194
    • Ostermeyer, A.G.1    Runko, E.2    Winkfield, B.3    Ahn, B.4    Moll, U.M.5
  • 46
    • 0034642549 scopus 로고    scopus 로고
    • Nuclear exclusion of p53 in a subset of tumors requires MDM2 function
    • Lu, W., et al. 2000. Nuclear exclusion of p53 in a subset of tumors requires MDM2 function. Oncogene. 19:232-240.
    • (2000) Oncogene , vol.19 , pp. 232-240
    • Lu, W.1
  • 47
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with mini-extracts, prepared from a small number of cells
    • Schreiber, E., Matthias, P., Muller, M.M., and Schaffner, W. 1989. Rapid detection of octamer binding proteins with mini-extracts, prepared from a small number of cells. Nucleic Acid Res. 17:6419-6420.
    • (1989) Nucleic Acid Res , vol.17 , pp. 6419-6420
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 48
    • 3042832606 scopus 로고    scopus 로고
    • Cell cycle regulation of NF-YC nuclear localization
    • Frontini, M., Imbriano, C., Manni, I., and Mantovani, R. 2004. Cell cycle regulation of NF-YC nuclear localization. Cell Cycle. 3:217-222.
    • (2004) Cell Cycle , vol.3 , pp. 217-222
    • Frontini, M.1    Imbriano, C.2    Manni, I.3    Mantovani, R.4
  • 49
    • 0027448548 scopus 로고
    • Inhibition of cell proliferation by an adenovirus vector expressing the human wild type p53 protein
    • Bacchetti, S., and Graham, F. 1993. Inhibition of cell proliferation by an adenovirus vector expressing the human wild type p53 protein. Int. J. Oncol. 3:781-788.
    • (1993) Int. J. Oncol , vol.3 , pp. 781-788
    • Bacchetti, S.1    Graham, F.2
  • 50
    • 0003412927 scopus 로고    scopus 로고
    • International Union Against Cancer, L.H. Sobin and Ch. Witteking, editors. Wilery-Liss. New York, New York, USA. 272 pp
    • International Union Against Cancer. 2002. TNM classification of malignant tumors. L.H. Sobin and Ch. Witteking, editors. Wilery-Liss. New York, New York, USA. 272 pp.
    • (2002) TNM classification of malignant tumors


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