Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding

Cell. 2007 Mar 9;128(5):841-52. doi: 10.1016/j.cell.2007.01.035.

Abstract

ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / metabolism*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Crystallography, X-Ray
  • Endosomal Sorting Complexes Required for Transport
  • Endosomes / metabolism
  • Gene Products, gag / metabolism
  • Glycoproteins / metabolism
  • HIV-1 / chemistry
  • HIV-1 / drug effects
  • HIV-1 / growth & development
  • HIV-1 / metabolism*
  • HeLa Cells
  • Humans
  • Infectious Anemia Virus, Equine / chemistry
  • Infectious Anemia Virus, Equine / growth & development
  • Infectious Anemia Virus, Equine / metabolism*
  • Models, Molecular
  • Mutation
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Viral Envelope Proteins / metabolism
  • gag Gene Products, Human Immunodeficiency Virus

Substances

  • Calcium-Binding Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Gene Products, gag
  • Glycoproteins
  • PDCD6IP protein, human
  • Recombinant Fusion Proteins
  • Viral Envelope Proteins
  • gag Gene Products, Human Immunodeficiency Virus
  • p6 gag protein, Human immunodeficiency virus 1