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c-Abl acetylation by histone acetyltransferases regulates its nuclear-cytoplasmic localization

Maria Giovanna di Bari1, Laura Ciuffini, Michele Mingardi

  • 1Dulbecco Telethon Institute, Via Montpellier 1, 00133 Rome, Italy.

EMBO Reports
|May 2, 2006
PubMed

Insights

Acetylation of c-Abl protein at Lys 730 drives its cytoplasmic accumulation during myogenic differentiation. This novel post-translational modification regulates c-Abl localization and promotes muscle cell development.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • c-Abl protein's function is regulated by its subcellular localization.
  • Histone acetyltransferases (HATs) like p300, CBP, and PCAF modify protein function through acetylation.

Purpose of the Study:

  • To investigate the role of acetylation in regulating c-Abl subcellular localization.
  • To identify the specific acetylation site responsible for altered c-Abl localization during myogenic differentiation.

Main Methods:

  • In vitro acetylation assays using purified c-Abl and HATs (p300, CBP, PCAF).
  • Point mutagenesis to identify key acetylation sites, specifically targeting Lysine 730 (Lys 730).
  • Analysis of c-Abl acetylation and localization during early stages of myogenic differentiation.

Main Results:

  • c-Abl is identified as a novel substrate for p300, CBP, and PCAF HATs.
  • Acetylation significantly alters c-Abl's subcellular localization.
  • Lys 730, within the second nuclear localization signal, is the primary site of p300-mediated acetylation.
  • Acetylation of Lys 730 drives c-Abl cytoplasmic accumulation during myogenic differentiation.

Conclusions:

  • Lys 730 acetylation represents a novel post-translational modification of c-Abl.
  • This acetylation mechanism modulates c-Abl's subcellular localization, impacting its function.
  • Lys 730 acetylation contributes to the process of myogenic differentiation.

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