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Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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Published on: March 3, 2016

Autoacetylation regulates P/CAF nuclear localization.

Noemí Blanco-García1, Elena Asensio-Juan, Xavier de la Cruz

  • 1Instituto de Biología Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Baldiri i Reixac 15-21, Parc Cientific de Barcelona, E-08028 Barcelona, Spain.

The Journal of Biological Chemistry
|November 19, 2008
PubMed
Summary

Protein acetylation, a key posttranslational modification, influences protein function. This study reveals how P/CAF autoacetylation controls its nuclear entry, impacting cellular processes like apoptosis.

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Assays for Validating Histone Acetyltransferase Inhibitors
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Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Acetylation is a crucial posttranslational modification regulating protein function.
  • The acetyltransferase P/CAF undergoes autoacetylation and acetylation by p300.
  • P/CAF autoacetylation affects protein localization and activity.

Purpose of the Study:

  • To investigate the role of P/CAF autoacetylation in regulating its subcellular distribution.
  • To understand the impact of deacetylation on P/CAF localization.
  • To explore the connection between P/CAF localization and apoptosis.

Main Methods:

  • Analysis of P/CAF mutants lacking histone acetyltransferase activity.
  • Assessment of P/CAF subcellular distribution following autoacetylation and deacetylation.
  • Investigation of P/CAF localization during apoptosis.

Main Results:

  • A P/CAF mutant lacking histone acetyltransferase activity accumulated in the cytoplasm.
  • Non-autoacetylated P/CAF was enriched in the cytoplasmic fraction.
  • Deacetylation by HDAC3, HDAC1, HDAC2, or HDAC4 led to cytoplasmic P/CAF accumulation.
  • P/CAF was observed to accumulate in the cytoplasm during apoptosis.

Conclusions:

  • Autoacetylation of P/CAF is a critical mechanism controlling its nuclear translocation.
  • Deacetylation by specific HDACs promotes P/CAF cytoplasmic localization.
  • P/CAF cytoplasmic accumulation during apoptosis suggests a novel regulatory pathway.