Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain

Nat Struct Mol Biol. 2006 Nov;13(11):1031-2. doi: 10.1038/nsmb1163. Epub 2006 Oct 22.

Abstract

ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Crystallography, X-Ray
  • Endosomal Sorting Complexes Required for Transport
  • Endosomes / metabolism
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Protein Transport
  • Saccharomyces cerevisiae Proteins / chemistry
  • Sequence Alignment
  • Transport Vesicles / metabolism*
  • Ubiquitin / chemistry
  • Ubiquitin / metabolism*
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / metabolism

Substances

  • Carrier Proteins
  • EAP45 protein, mouse
  • Endosomal Sorting Complexes Required for Transport
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • Vesicular Transport Proteins
  • Vps36 protein, S cerevisiae

Associated data

  • PDB/2DX5