1,284
Views
34
CrossRef citations to date
0
Altmetric
Research Paper

Wild-type and mutant p53 proteins interact with mitochondrial caspase-3

, , , &
Pages 740-745 | Received 01 Dec 2010, Accepted 21 Jan 2011, Published online: 15 Apr 2011

References

  • Nicholson DW. Caspase structure, proteolytic substrates and function during apoptotic death. Cell Death Differ 1999; 6:1028 - 1042
  • Stennicke HR, Salvesen GS. Properties of the caspases. Biochimica et Biophysica Acta 1998; 1387:17 - 31
  • Taylor RC, Cullen SP, Martin SJ. Apoptosis: controlled demolition at the cellular level. Nat Rev Mol Cell Biol 2008; 9:231 - 241
  • Zhivotovsky B, Samali A, Gahm A, Orrenius S. Caspases: their intracellular localization and translocation during apoptosis. Cell Death Differ 1999; 6:644 - 651
  • Samali A, Zhivotovsky B, Jones DP, Orrenius S. Detection of pro-caspase-3 in cytosol and mitochondria of various tissues. FEBS 1998; 431:167 - 169
  • Mancini M, Nicholson DW, Roy S, Thornberry NA, Peterson EP, Casciola-Rosen LA, et al. The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling. J Cell Biol 1998; 140:1485 - 1495
  • Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S. Presence of a pre-apoptotic complex of pro-caspse-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J 1999; 18:2040 - 2048
  • Levine AJ. p53, the cellular gatekeeper for growth and division. Cell 1997; 88:323 - 331
  • Mihara M, Erster S, Zaika A, Petrenko O, Chittenden T, Pancoska P, et al. p53 has a direct apoptogenic role at the mitochondria. Mol Cell 2003; 11:577 - 590
  • Chipuk J, Kuwana T, Bouchier-Hayes L, Droin N, Newmeyer D, Schuler M, et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004; 303:1010 - 1014
  • Leu J, Dumont P, Hafey M, Murphy M, George D. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nat Cell Biol 2004; 6:443 - 450
  • Pietsch EEP, Canutescu A, Wang G, Dunbrack R, Murphy M. Oligomerization of BAK by p53 utilizes conserved residues of the p53 DNA binding domain. J Biol Chem 2008; 283:21294 - 21304
  • Cho Y, Gorina S, Jeffrey P, Pavletich N. Crystal structure of a p53 tumor suppressor-DNA complex: uncerstanding tumorigenic mutations. Science 1994; 265:346 - 355
  • Hollstein M, Sidransky D, Vogelstein B, Harris C. p53 mutations in human cancers. Science 1991; 253:49 - 53
  • Tomita Y, Marchenko N, Erster S, Nemajerova A, Dehner A, Klein C, et al. WT p53, but not tumor-derived mutants, bind to Bcl2 via the DNA binding domain and induce mitochondrial permeabilization. J Biol Chem 2006; 28:8600 - 8606
  • Sayan BS, Sayan AE, Knight RA, Melino G, Cohen GM. p53 is cleaved by caspases generating fragments localizing to mitochondria. J Biol Chem 2006; 281:13566 - 13573
  • Zambetti GP, Levine AJ. A comparison of the biological activities of wild-type and mutant p53. FASEB J 1993; 7:855 - 865
  • Marin MC, Jost CA, Brooks LA, Irwin MS, O'Nions J, Tidy JA, et al. A common polymorphism acts as an intragenic modifier of mutant p53 behaviour. Nat Genet 2000; 25:47 - 54
  • Song H, Hollstein M, Xu Y. p53 gain-of-function cancer mutants induce genetic instability by inactivating ATM. Nat Cell Biol 2007; 9:573 - 580
  • Pimkina J, Humbey O, Zilfou JT, Jarnik M, Murphy ME. ARF induces autophagy by virtue of interaction with Bcl-xl. J Biol Chem 2009; 284:2803 - 2810

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.