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Pore-forming activity of BAD is regulated by specific phosphorylation and structural transitions of the C-terminal

Lisa Polzien1, Angela Baljuls, Heide-Marie Roth

  • 1Theodor Boveri Institute, Department of Microbiology, University of Wuerzburg, 97074 Wuerzburg, Germany. lisa.polzien@uni-wuerzburg.de

Biochimica Et Biophysica Acta
|November 18, 2010
PubMed
Abstract

Insights

The C-terminal region of BAD protein regulates cell death by controlling its structure, lipid binding, and phosphorylation. This region

Area of Science:

  • * Molecular biology
  • * Cell death regulation
  • * Protein structure-function relationships

Background:

  • * BAD protein, a BH3-only proapoptotic factor, acts as a cellular health sentinel.
  • * Its activity is modulated by phosphorylation, 14-3-3 binding, lipid interactions, and pore formation.
  • * The C-terminal region's role in BAD function remains largely unexplored.

Purpose of the Study:

  • * To investigate the structure-function interplay of the BAD C-terminal region.
  • * To elucidate the role of C-terminal structural transitions in BAD-mediated cell death.

Main Methods:

  • * Circular dichroism (CD) spectroscopy for structural analysis.
  • * Lipid bilayer measurements for channel-forming activity.
  • * Surface plasmon resonance (SPR) for protein-peptide interactions.

Main Results:

  • * The BAD C-terminus exhibits a stable structure in solution, with increased helical propensity in a lipid environment.
  • * Phosphorylation at serine 118 is crucial for pore formation, while phosphorylation at serine 99 inhibits it.
  • * The C-terminal region controls BAD function through structural changes, lipid binding, and phosphorylation.

Conclusions:

  • * The C-terminal region of BAD is a key regulator of its proapoptotic function.
  • * Conformational changes and phosphorylation within this region dictate BAD's interaction with membranes and its role in cell death pathways.

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