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RPL24: a potential therapeutic target whose depletion or acetylation inhibits polysome assembly and cancer cell

Kathleen A Wilson-Edell1, Amanuel Kehasse1, Gary K Scott1

  • 1Buck Institute for Research on Aging; Novato, CA, USA.

Oncotarget
|June 28, 2014
PubMed

Insights

Large ribosomal subunit protein 24 (RPL24) is elevated in breast cancer, driving tumor growth by promoting translation of key proteins. Inhibiting RPL24 or its acetylation may offer new cancer therapies.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • Partial loss of large ribosomal subunit protein 24 (RPL24) confers protection against Akt or Myc-driven cancers in mice.
  • RPL24's role in human malignancies, particularly breast cancer, remains largely unknown.

Purpose of the Study:

  • To investigate the role of RPL24 in human breast cancer.
  • To explore the impact of RPL24 depletion on breast cancer cell viability and protein expression.
  • To elucidate the mechanism of RPL24 regulation, focusing on acetylation and its effect on ribosome assembly.

Main Methods:

  • Analysis of public human breast cancer and normal mammary tissue datasets.
  • RPL24 depletion in breast cancer cells using knockdown techniques.
  • Assessment of cell viability and specific protein expression levels (cyclin D1, survivin, NBS1, GAPDH, beta-tubulin).
  • Investigation of the effects of pan-histone deacetylase inhibitor (trichostatin A) and HDAC6 inhibition/knockdown.
  • Mass spectrometry to identify acetylated proteins, including RPL24.

Main Results:

  • Breast cancers exhibit significantly higher RPL24 expression compared to normal tissue.
  • RPL24 depletion (>70%) drastically reduced breast cancer cell viability (80%) and decreased key oncogenic protein levels.
  • RPL24 knockdown affected 80S ribosome subunit levels and mimicked effects of trichostatin A treatment.
  • Histone deacetylase inhibition (HDACi) induced acetylation of RPL24 on K27, particularly in 60S-associated RPL24.

Conclusions:

  • RPL24 is upregulated in human breast cancer and contributes to tumorigenesis.
  • RPL24 acetylation, potentially regulated by HDAC6, plays a role in ribosome assembly and cancer progression.
  • Targeting RPL24 or its acetylation presents a novel therapeutic strategy for breast cancer.

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