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The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
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Related Experiment Video

Updated: May 15, 2026

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death
09:18

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

Published on: December 27, 2016

Bak apoptotic function is not directly regulated by phosphorylation.

V H Tran1, R Bartolo, D Westphal

  • 1Molecular Genetics of Cancer Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.

Cell Death & Disease
|January 11, 2013
PubMed
Summary
This summary is machine-generated.

Bak protein activation during apoptosis does not rely on dephosphorylation. Studies show Bak is not significantly phosphorylated, and altering phosphorylation sites does not affect its pro-apoptotic function.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Bak and Bax proteins are crucial for apoptosis, inducing mitochondrial outer membrane permeabilization.
  • Bak activation involves conformational changes and oligomerization.
  • Previous research suggested Bak activation requires dephosphorylation of tyrosine-108.

Purpose of the Study:

  • To investigate the role of Bak phosphorylation and dephosphorylation in its activation during apoptosis.
  • To determine if dephosphorylation of specific sites, like tyrosine-108, is necessary for Bak function.

Main Methods:

  • One-dimensional isoelectric focusing (1D-IEF) was used to analyze Bak phosphorylation status.
  • Mutagenesis, including alanine substitution of tyrosine-108 and other putative sites, was employed.
  • Engineered 'phosphotagged' Bak variants were created to detect phosphorylation.

Main Results:

  • 1D-IEF analysis showed Bak exists as a single band, indicating no significant phosphorylation across various cell types, even after phosphatase treatment.
  • Engineered phosphotagged Bak variants exhibited a second band, confirming the detection method for phosphorylation.
  • Apoptosis induction did not alter Bak's isoelectric point, suggesting no significant change in its phosphorylation status.
  • Mutating tyrosine-108 and other potential phosphorylation sites did not enhance Bak activation or pro-apoptotic activity.

Conclusions:

  • Bak protein is not significantly phosphorylated in cells.
  • Bak activation during apoptosis does not require dephosphorylation of tyrosine-108 or other identified sites.
  • The proposed model of Bak activation requiring dephosphorylation is not supported by these findings.