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Volumn 364, Issue 2, 2007, Pages 344-350

PLAGL2 controls the stability of Pirh2, an E3 ubiquitin ligase for p53

Author keywords

Dimer stability; Pirh2; PLAGL2

Indexed keywords

ONCOPROTEIN; PROTEIN P53; PROTEIN PIRH2; PROTEIN PLAGL2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 35448998867     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.003     Document Type: Article
Times cited : (26)

References (33)
  • 1
    • 0032483441 scopus 로고    scopus 로고
    • Transcriptional activation capacity of the novel PLAG family of zinc finger proteins
    • Kas K., Voz M.L., Hensen K., Meyen E., and Van de Ven W.J. Transcriptional activation capacity of the novel PLAG family of zinc finger proteins. J. Biol. Chem. 273 (1998) 23026-23032
    • (1998) J. Biol. Chem. , vol.273 , pp. 23026-23032
    • Kas, K.1    Voz, M.L.2    Hensen, K.3    Meyen, E.4    Van de Ven, W.J.5
  • 3
    • 0034849520 scopus 로고    scopus 로고
    • PLAG1 alterations in lipoblastoma: involvement in varied mesenchymal cell types and evidence for alternative oncogenic mechanisms
    • Gisselsson D., Hibbard M.K., Dal Cin P., Sciot R., Hsi B.L., Kozakewich H.P., and Fletcher J.A. PLAG1 alterations in lipoblastoma: involvement in varied mesenchymal cell types and evidence for alternative oncogenic mechanisms. Am. J. Pathol. 159 (2001) 955-962
    • (2001) Am. J. Pathol. , vol.159 , pp. 955-962
    • Gisselsson, D.1    Hibbard, M.K.2    Dal Cin, P.3    Sciot, R.4    Hsi, B.L.5    Kozakewich, H.P.6    Fletcher, J.A.7
  • 5
    • 2542508022 scopus 로고    scopus 로고
    • Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene
    • Astrom A.K., Voz M.L., Kas K., Roijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., and Stenman G. Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene. Cancer Res. 59 (1999) 918-923
    • (1999) Cancer Res. , vol.59 , pp. 918-923
    • Astrom, A.K.1    Voz, M.L.2    Kas, K.3    Roijer, E.4    Wedell, B.5    Mandahl, N.6    Van de Ven, W.7    Mark, J.8    Stenman, G.9
  • 8
    • 0036494660 scopus 로고    scopus 로고
    • The tumorigenic diversity of the three PLAG family members is associated with different DNA binding capacities
    • Hensen K., Van Valckenborgh I.C., Kas K., Van de Ven W.J., and Voz M.L. The tumorigenic diversity of the three PLAG family members is associated with different DNA binding capacities. Cancer Res. 62 (2002) 1510-1517
    • (2002) Cancer Res. , vol.62 , pp. 1510-1517
    • Hensen, K.1    Van Valckenborgh, I.C.2    Kas, K.3    Van de Ven, W.J.4    Voz, M.L.5
  • 10
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 88 (1997) 323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 11
    • 0037309326 scopus 로고    scopus 로고
    • Tumor suppression by Ink4a-Arf: progress and puzzles
    • Lowe S.W., and Sherr C.J. Tumor suppression by Ink4a-Arf: progress and puzzles. Curr. Opin. Genet. Dev. 13 (2003) 77-83
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 77-83
    • Lowe, S.W.1    Sherr, C.J.2
  • 12
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation
    • Brooks C.L., and Gu W. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15 (2003) 164-171
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 14
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y., Wolf G.W., Bhat K., Jin A., Allio T., Burkhart W.A., and Xiong Y. Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell. Biol. 23 (2003) 8902-8912
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 15
    • 0035852716 scopus 로고    scopus 로고
    • A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control
    • Li L., Liao J., Ruland J., Mak T.W., and Cohen S.N. A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control. Proc. Natl. Acad. Sci. USA 98 (2001) 1619-1624
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1619-1624
    • Li, L.1    Liao, J.2    Ruland, J.3    Mak, T.W.4    Cohen, S.N.5
  • 16
    • 11844301301 scopus 로고    scopus 로고
    • Regulation of p53 and MDM2 activity by MTBP
    • Brady M., Vlatkovic N., and Boyd M.T. Regulation of p53 and MDM2 activity by MTBP. Mol. Cell. Biol. 25 (2005) 545-553
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 545-553
    • Brady, M.1    Vlatkovic, N.2    Boyd, M.T.3
  • 19
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M., Huibregtse J.M., Vierstra R.D., and Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75 (1993) 495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 21
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • Chen D., Kon N., Li M., Zhang W., Qin J., and Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121 (2005) 1071-1083
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 23
    • 34548169288 scopus 로고    scopus 로고
    • The ORF3 protein of porcine circovirus type 2 interacts with porcine ubiquitin E3 ligase Pirh2 and facilitates p53 expression in viral infection
    • Liu J., Zhu Y., Chen I., Lau J., He F., Lau A., Wang Z., Karuppannan A.K., and Kwang J. The ORF3 protein of porcine circovirus type 2 interacts with porcine ubiquitin E3 ligase Pirh2 and facilitates p53 expression in viral infection. J. Virol. 81 (2007) 9560-9567
    • (2007) J. Virol. , vol.81 , pp. 9560-9567
    • Liu, J.1    Zhu, Y.2    Chen, I.3    Lau, J.4    He, F.5    Lau, A.6    Wang, Z.7    Karuppannan, A.K.8    Kwang, J.9
  • 24
    • 1642523726 scopus 로고    scopus 로고
    • Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome
    • Logan I.R., Sapountzi V., Gaughan L., Neal D.E., and Robson C.N. Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome. J. Biol. Chem. 279 (2004) 11696-11704
    • (2004) J. Biol. Chem. , vol.279 , pp. 11696-11704
    • Logan, I.R.1    Sapountzi, V.2    Gaughan, L.3    Neal, D.E.4    Robson, C.N.5
  • 25
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • Nikolay R., Wiederkehr T., Rist W., Kramer G., Mayer M.P., and Bukau B. Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279 (2004) 2673-2678
    • (2004) J. Biol. Chem. , vol.279 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 26
    • 1442330336 scopus 로고    scopus 로고
    • S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity
    • Ravi K., Brennan L.A., Levic S., Ross P.A., and Black S.M. S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity. Proc. Natl. Acad. Sci. USA 101 (2004) 2619-2624
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2619-2624
    • Ravi, K.1    Brennan, L.A.2    Levic, S.3    Ross, P.A.4    Black, S.M.5
  • 27
    • 0032563319 scopus 로고    scopus 로고
    • Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
    • Johnson P.R., Swanson R., Rakhilina L., and Hochstrasser M. Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 94 (1998) 217-227
    • (1998) Cell , vol.94 , pp. 217-227
    • Johnson, P.R.1    Swanson, R.2    Rakhilina, L.3    Hochstrasser, M.4
  • 28
    • 0034625366 scopus 로고    scopus 로고
    • Ubiquitination of neuronal nitric-oxide synthase in vitro and in vivo
    • Bender A.T., Demady D.R., and Osawa Y. Ubiquitination of neuronal nitric-oxide synthase in vitro and in vivo. J. Biol. Chem. 275 (2000) 17407-17411
    • (2000) J. Biol. Chem. , vol.275 , pp. 17407-17411
    • Bender, A.T.1    Demady, D.R.2    Osawa, Y.3
  • 29
    • 0037422171 scopus 로고    scopus 로고
    • C/EBP family transcription factors are degraded by the proteasome but stabilized by forming dimer
    • Hattori T., Ohoka N., Inoue Y., Hayashi H., and Onozaki K. C/EBP family transcription factors are degraded by the proteasome but stabilized by forming dimer. Oncogene 22 (2003) 1273-1280
    • (2003) Oncogene , vol.22 , pp. 1273-1280
    • Hattori, T.1    Ohoka, N.2    Inoue, Y.3    Hayashi, H.4    Onozaki, K.5
  • 30
    • 0029092658 scopus 로고
    • Neuronal nitric oxide synthase self-inactivates by forming a ferrous-nitrosyl complex during aerobic catalysis
    • Abu-Soud H.M., Wang J., Rousseau D.L., Fukuto J.M., Ignarro L.J., and Stuehr D.J. Neuronal nitric oxide synthase self-inactivates by forming a ferrous-nitrosyl complex during aerobic catalysis. J. Biol. Chem. 270 (1995) 22997-23006
    • (1995) J. Biol. Chem. , vol.270 , pp. 22997-23006
    • Abu-Soud, H.M.1    Wang, J.2    Rousseau, D.L.3    Fukuto, J.M.4    Ignarro, L.J.5    Stuehr, D.J.6
  • 31
    • 0029935269 scopus 로고    scopus 로고
    • Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability
    • Albakri Q.A., and Stuehr D.J. Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability. J. Biol. Chem. 271 (1996) 5414-5421
    • (1996) J. Biol. Chem. , vol.271 , pp. 5414-5421
    • Albakri, Q.A.1    Stuehr, D.J.2
  • 32
    • 0033569879 scopus 로고    scopus 로고
    • An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity
    • Ratovitski E.A., Bao C., Quick R.A., McMillan A., Kozlovsky C., and Lowenstein C.J. An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity. J. Biol. Chem. 274 (1999) 30250-30257
    • (1999) J. Biol. Chem. , vol.274 , pp. 30250-30257
    • Ratovitski, E.A.1    Bao, C.2    Quick, R.A.3    McMillan, A.4    Kozlovsky, C.5    Lowenstein, C.J.6


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