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1.
FIGURE 4.

FIGURE 4. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

Lys-382 acetylation does not occur on p53 mutant that is incapable of forming oligomers. H1299 cells were transiently transfected with indicated p53 plasmids for 24 h. Cell lysates were analyzed with the indicated antibodies. GFP was used as a control for transfection efficiency.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
2.
FIGURE 3.

FIGURE 3. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

p53 NES mutant is defective in oligomerization. Cell lysates expressing wild-type p53 and each of the indicated p53 mutants were incubated on ice with glutaraldehyde at the indicated concentrations for 20 min. The samples were resolved on SDS-polyacrylamide gel and blotted with p53 antibody (DO-1). The molecular weight marker and the positions of monomer, dimer, and tetramer p53 are indicated.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
3.
FIGURE 6.

FIGURE 6. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

The acetyltransferase p300 interacts with and promotes acetylation of wild-type p53, but not with mutant p53 that are defective in oligomerization. A, interaction of p53 with p300 was tested by co-immunoprecipitation from the cell lysate of H1299 transiently transfected with plasmids encoding HA-p300 and various p53 as indicated. The lysates were immunoprecipitated with anti-HA antibody and blotted with the indicated antibodies. B, p300 promotes acetylation of p53 that are able to form tetramers. H1299 cells were transiently transfected with plasmids encoding HA-p300 and various p53 as indicated for 24 h. Cell lysates were analyzed by Western blotting with the indicated antibodies.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
4.
FIGURE 7.

FIGURE 7. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

A model for p53 activation. A, model for sequential and stepwise activation of p53. DNA damage induces formation of p53 tetramer, which provides docking sites for p300, leading to p300 binding and subsequent acetylation of p53. The acetylation of p53 further tightens the p300-p53 complex, stabilizes p53, and facilitates recruitment of co-activators leading to transactivation of p53 target genes. B–D, ribbon diagram of p53 tetramer and dimer (constructed from the Protein Data Bank entry 1C26). The hydrophobic residues analyzed in the study are indicated in red. Residues tested by mutational analysis are indicated by arrows.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
5.
FIGURE 2.

FIGURE 2. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

Restoration of nuclear export function of p53NES mutant cannot restore Lys-382 acetylation. A, acetylation of nuclear confined p53. H1299 cells were transiently transfected with indicated p53 plasmids. One day after transfection, the cells were treated with 0.5 μm TSA plus 5 mm nicotinamide (Nico) in the absence (lanes 1, 3, and 5) or presence (lanes 2, 4, and 6) of 10 nm LMB for 1 day before lysis. p53 acetylation was analyzed by Western blotting using antibody to Lys-382 acetylated p53. B, restoration of nuclear export function of p53NES mutant cannot restore Lys-382 acetylation. H1299 cells were transiently transfected with indicated p53 plasmids. The cells were then treated without (lanes 1–4) or with (lanes 5–8) 0.5 μm TSA plus 5 mm nicotinamide (Nico) for 6 h before lysis. p53 acetylation was analyzed by Western blotting using antibody to Lys-382 acetylated p53.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
6.
FIGURE 5.

FIGURE 5. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

Cancer-associated p53 mutants are defective in oligomerization, acetylation, and transactivation. A, oligomer formation of wild-type p53 and two cancer-associated p53 mutants, L344P and R337C. H1299 cells were transiently transfected with indicated plasmid DNA for 24 h. Cell lysates were examined for p53 oligomerization by a protein cross-linking assay. B, cancer-associated p53 oligomer mutants are deficient in Lys-382 acetylation and p21 transactivation. H1299 cells were transiently transfected with plasmids expressing wild-type, L344P, or R337C mutant p53, and the cell lysates were blotted with the indicated antibodies. GFP was used as a control for transfection efficiency. C, p53 oligomer mutants are deficient in acetylation on multiple C-terminal lysine residues determined by a pan-Ace-p53 antibody that recognizes acetylated lysines at position Lys-372, Lys-373, Lys-381, and Lys-382 ().

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.
7.
FIGURE 1.

FIGURE 1. From: p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation.

Nucleus-confined but not cytoplasm-confined p53 is defective in Lys-382 acetylation. A, diagram of human p53 protein with amino acid sequences of the bipartite NLS and the C-terminal NES indicated. The functionally important basic amino acid residues in the NLS and hydrophobic amino acid residues in the NES are shown in boldface in the wild-type (WT) sequence. Alanine substitutions in the p53 mutants are indicated. B, localization of wild-type and mutant p53 proteins. U2OS cells were transiently transfected with plasmid DNA expressing indicated p53 proteins. Fluorescence and phase contrast images were taken 24 h after transfection. C, detection of p53 acetylation at Lys-382. H1299 cells were transiently transfected with indicated p53 plasmid DNA. Cell lysates were collected 24 h after transfection, immunoprecipitated by anti-p53 antibody, and resolved on SDS-polyacrylamide gel and blotted with antibodies specific to Lys-382 acetylated p53 (Ace382), p53, and actin.

Yoko Itahana, et al. J Biol Chem. 2009 February 20;284(8):5158-5164.

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