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Volumn 17, Issue 10, 2008, Pages 1663-1670

Members of the S100 family bind p53 in two distinct ways

Author keywords

Negative regulatory domain; p53; Protein protein interactions; S100 proteins; Tetramerization

Indexed keywords

CALCYCLIN; CALVASCULIN; PROTEIN P53; PROTEIN S 100; PROTEIN S100 A1; PROTEIN S100 A11; PROTEIN S100 A2; PROTEIN S100B; UNCLASSIFIED DRUG;

EID: 52949152903     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.035527.108     Document Type: Article
Times cited : (74)

References (26)
  • 1
    • 0026437598 scopus 로고
    • Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein
    • Baudier, J., Delphin, C., Grunwald, D., Khochbin, S., and Lawrence, J.J. 1992. Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein. Proc. Natl. Acad. Sci. 89: 11627-11631.
    • (1992) Proc. Natl. Acad. Sci , vol.89 , pp. 11627-11631
    • Baudier, J.1    Delphin, C.2    Grunwald, D.3    Khochbin, S.4    Lawrence, J.J.5
  • 3
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 5
    • 0032983595 scopus 로고    scopus 로고
    • Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type
    • Donato, R. 1999. Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type. Biochim. Biophys. Acta 1450: 191-231.
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 191-231
    • Donato, R.1
  • 6
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato, R. 2001. S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33: 637-668.
    • (2001) Int. J. Biochem. Cell Biol , vol.33 , pp. 637-668
    • Donato, R.1
  • 7
    • 0027203055 scopus 로고
    • Six S100 genes are clustered on human chromosome 1q21: Identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E
    • Engelkamp, D., Schafer, B.W., Mattei, M.G., Erne, P., and Heizmann, C.W. 1993. Six S100 genes are clustered on human chromosome 1q21: Identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. Proc. Natl. Acad. Sci. 90: 6547-6551.
    • (1993) Proc. Natl. Acad. Sci , vol.90 , pp. 6547-6551
    • Engelkamp, D.1    Schafer, B.W.2    Mattei, M.G.3    Erne, P.4    Heizmann, C.W.5
  • 8
    • 16344368267 scopus 로고    scopus 로고
    • Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor
    • Fernandez-Fernandez, M.R., Veprintsev, D.B., and Fersht, A.R. 2005. Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor. Proc. Natl. Acad. Sci. 102: 4735-4740.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 4735-4740
    • Fernandez-Fernandez, M.R.1    Veprintsev, D.B.2    Fersht, A.R.3
  • 9
    • 0033534740 scopus 로고    scopus 로고
    • Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization
    • Garbuglia, M., Verzini, M., Rustandi, R.R., Osterloh, D., Weber, D.J., Gerke, V., and Donato, R. 1999. Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization. Biochem. Biophys. Res. Commun. 254: 36-41.
    • (1999) Biochem. Biophys. Res. Commun , vol.254 , pp. 36-41
    • Garbuglia, M.1    Verzini, M.2    Rustandi, R.R.3    Osterloh, D.4    Weber, D.J.5    Gerke, V.6    Donato, R.7
  • 12
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • Kassam, G., Le, B.H., Choi, K.S., Kang, H.M., Fitzpatrick, S.L., Louie, P., and Waisman, D.M. 1998. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry 37: 16958-16966.
    • (1998) Biochemistry , vol.37 , pp. 16958-16966
    • Kassam, G.1    Le, B.H.2    Choi, K.S.3    Kang, H.M.4    Fitzpatrick, S.L.5    Louie, P.6    Waisman, D.M.7
  • 13
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A.J. 1997. p53, the cellular gatekeeper for growth and division. Cell 88: 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 14
    • 0035860784 scopus 로고    scopus 로고
    • Inhibition of p53 transcriptional activity by the S100B calcium-binding protein
    • Lin, J., Blake, M., Tang, C., Zimmer, D., Rustandi, R.R., Weber, D.J., and Carrier, F. 2001. Inhibition of p53 transcriptional activity by the S100B calcium-binding protein. J. Biol. Chem. 276: 35037-35041.
    • (2001) J. Biol. Chem , vol.276 , pp. 35037-35041
    • Lin, J.1    Blake, M.2    Tang, C.3    Zimmer, D.4    Rustandi, R.R.5    Weber, D.J.6    Carrier, F.7
  • 15
    • 0032525133 scopus 로고    scopus 로고
    • Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain
    • Mateu, M.G. and Fersht, A.R. 1998. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. EMBO J. 17: 2748-2758.
    • (1998) EMBO J , vol.17 , pp. 2748-2758
    • Mateu, M.G.1    Fersht, A.R.2
  • 16
    • 0030593468 scopus 로고    scopus 로고
    • Overproduction of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. and Walker, J.E. 1996. Overproduction of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260: 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 17
    • 23844505646 scopus 로고    scopus 로고
    • The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity
    • Mueller, A., Schafer, B.W., Ferrari, S., Weibel, M., Makek, M., Hochli, M., and Heizmann, C.W. 2005. The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity. J. Biol. Chem. 280: 29186-29193.
    • (2005) J. Biol. Chem , vol.280 , pp. 29186-29193
    • Mueller, A.1    Schafer, B.W.2    Ferrari, S.3    Weibel, M.4    Makek, M.5    Hochli, M.6    Heizmann, C.W.7
  • 18
  • 21
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(ββ)
    • Rustandi, R.R., Baldisseri, D.M., and Weber, D.J. 2000. Structure of the negative regulatory domain of p53 bound to S100B(ββ). Nat. Struct. Biol. 7: 570-574.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 22
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schafer, B.W. and Heizmann, C.W. 1996. The S100 family of EF-hand calcium-binding proteins: Functions and pathology. Trends Biochem. Sci. 21: 134-140.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 134-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 23
    • 0031834812 scopus 로고    scopus 로고
    • Calcium and S100B regulation of p53-dependent cell growth arrest and apoptosis
    • Scotto, C., Deloulme, J.C., Rousseau, D., Chambaz, E., and Baudier, J. 1998. Calcium and S100B regulation of p53-dependent cell growth arrest and apoptosis. Mol. Cell. Biol. 18: 4272-4281.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4272-4281
    • Scotto, C.1    Deloulme, J.C.2    Rousseau, D.3    Chambaz, E.4    Baudier, J.5
  • 24
    • 0032862991 scopus 로고    scopus 로고
    • Concerted regulation of wild-type p53 nuclear accumulation and activation by S100B and calcium-dependent protein kinase C
    • Scotto, C., Delphin, C., Deloulme, J.C., and Baudier, J. 1999. Concerted regulation of wild-type p53 nuclear accumulation and activation by S100B and calcium-dependent protein kinase C. Mol. Cell. Biol. 19: 7168-7180.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7168-7180
    • Scotto, C.1    Delphin, C.2    Deloulme, J.C.3    Baudier, J.4
  • 25
    • 0034703742 scopus 로고    scopus 로고
    • Death star
    • p53
    • Vousden, K.H. 2000. p53: Death star. Cell 103: 691-694.
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.