Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain.
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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, Endosomes, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Protein Transport, Saccharomyces cerevisiae Proteins, Sequence Alignment, Transport Vesicles, Ubiquitin, Vesicular Transport Proteins
Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, Endosomes, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Protein Transport, Saccharomyces cerevisiae Proteins, Sequence Alignment, Transport Vesicles, Ubiquitin, Vesicular Transport Proteins
Nat. Struct. Mol. Biol.
Date: Nov. 01, 2006
PubMed ID: 17057714
View in: Pubmed Google Scholar
Download Curated Data For This Publication
69270
Switch View:
- Interactions 2