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Updated: Jul 20, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
10:55

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Oligomerization of p53 precedes its association with dynein and nuclear accumulation

Shana Y Trostel1, Dan L Sackett, Tito Fojo

  • 1Medical Oncology Branch, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA.

Cell Cycle (Georgetown, Tex.)
|September 14, 2006
PubMed

Insights

The p53 protein forms oligomers that bind to dynein motors for nuclear transport. Mutations affecting p53 oligomerization disrupt this process and alter cellular distribution.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Proteins like p53, glucocorticoid receptors, vitamin D receptors, and APC associate with microtubules and dynein.
  • The specific protein residues and physical states involved in these interactions remain unclear.

Purpose of the Study:

  • To identify the crucial residues and physical state of p53 involved in dynein motor complex association and nuclear transport.
  • To elucidate the mechanism of p53 intracellular trafficking.

Main Methods:

  • Utilized SN12C cells with mutant p53 (truncated at amino acid 336).
  • Examined a series of truncated p53 proteins and point mutations.
  • Investigated p53 association with dynein and microtubules in cytosolic and nuclear fractions.

Main Results:

  • Truncated p53 (at amino acid 336) showed impaired nuclear localization and dynein binding.
  • Residues 336-348 of p53 are critical for dynein association and nuclear transport.
  • p53 oligomerization is essential for its function as cargo for dynein transport.
  • Cytosolic p53 oligomers bind dynein independently of microtubules, followed by microtubule association for transport.

Conclusions:

  • p53 oligomerization is crucial for its dynein-mediated nuclear transport and intracellular distribution.
  • Mutations affecting p53 oligomerization impact both DNA binding and cellular localization.
  • An intact microtubule network is vital for the trafficking of essential cellular proteins like p53.

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