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Related Experiment Video

Updated: Jul 14, 2025

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

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Published on: December 27, 2016

Acetylation-dependent coupling between G6PD activity and apoptotic signaling.

Fang Wu¹, Natali H Muskat¹, Inbar Dvilansky²

¹Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, 8410501, Israel.

Nature Communications

|October 5, 2023

Summary

This summary is machine-generated.

Lysine acetylation regulates metabolic enzymes like glucose-6-phosphate dehydrogenase (G6PD). This modification can activate or inhibit G6PD, impacting cellular signaling and apoptosis.

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Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

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Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c

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Published on: June 29, 2011

Area of Science:

Biochemistry
Molecular Biology
Cellular Signaling

Background:

Lysine acetylation is a widespread posttranslational modification in human proteins, including metabolic enzymes.
Understanding acetylation's role is crucial for elucidating metabolic regulation and cellular communication.

Purpose of the Study:

To investigate the functional impact of lysine acetylation on glucose-6-phosphate dehydrogenase (G6PD).
To explore how G6PD acetylation influences its enzymatic activity, downstream modifications, and cellular processes like apoptosis.

Main Methods:

Utilized site-specifically acetylated G6PD for functional analysis.
Employed structural studies to elucidate mechanisms of acetylation-dependent inhibition.
Investigated acetylation-dependent ubiquitylation, phosphorylation, and protein interactions.

Main Results:

Acetylation at K89 activates G6PD, while acetylation at K403 inhibits it.
Acetylation-induced G6PD inactivation involves structural distortion of the enzyme's active site.
Demonstrated acetylation-dependent ubiquitylation (K95/97), phosphorylation (Y503), p53 interaction, and induction of apoptosis.

Conclusions:

A single lysine acetylation site can coordinate multiple acetylation-dependent events.
Acetylation is a complex posttranslational modification regulating enzymatic activity, further modifications, and apoptotic signaling pathways.