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ALIX-CHMP4 interactions in the human ESCRT pathway.

John McCullough1, Robert D Fisher, Frank G Whitby

  • 1Department of Biochemistry, University of Utah, Salt Lake City, UT 84112-5650, USA.

Proceedings of the National Academy of Sciences of the United States of America
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Summary

The ALIX protein binds CHMP4 proteins, crucial for HIV budding and cell division. Distinct hydrophobic residue patterns on CHMP4 act as a code, dictating specific binding interactions within the ESCRT pathway.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Virology

Background:

  • The ESCRT pathway is vital for membrane fission in processes like viral budding and cytokinesis.
  • ALIX protein recruits CHMP4 subunits of ESCRT-III for membrane remodeling during HIV budding and cell division.

Purpose of the Study:

  • To elucidate the structural basis of ALIX-CHMP4 interaction.
  • To understand how specific binding codes regulate ESCRT-III subunit interactions.

Main Methods:

  • X-ray crystallography to determine the structure of ALIX(Bro1) bound to CHMP4 peptides.
  • Site-directed mutagenesis to investigate the role of specific residues in ALIX-CHMP4 binding and HIV budding.

Main Results:

  • ALIX's Bro1 domain specifically binds C-terminal amphipathic helices of CHMP4 proteins.
  • Crystal structures reveal CHMP4 peptides binding to the concave surface of ALIX(Bro1).
  • Mutations in key ALIX(Bro1) residues disrupt binding to CHMP4 and block HIV-1 budding.

Conclusions:

  • A hydrophobic residue pattern (M/L/IxxLxxW) on CHMP4 recognition helix dictates binding to ALIX.
  • Distinct hydrophobic spacing in CHMP1-3 (L/I/MxxxLxxL) allows binding to other ESCRT partners like VPS4 and Vta1/LIP5.
  • This 'code' ensures specificity in ESCRT-III subunit interactions for diverse cellular functions.