Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover.
Nbr1, a ubiquitous kinase scaffold protein, contains a PB1, and a ubiquitin-associated (UBA) domain. We show here that the nbr1 UBA domain binds to lysine-48 and -63 linked polyubiquitin-B chains. Nbr1 also binds to the autophagic effector protein LC3-A via a novel binding site. Ubiquitin-binding, but not PB1-mediated p62/SQSTM1 interaction, ... is required to target nbr1 to LC3 and polyubiquitin-positive bodies. Nbr1 binds additionally to proteins implicated in ubiquitin-mediated protein turnover and vesicle trafficking: ubiquitin-specific peptidases USP8, and the endosomal transport regulator p14/Robld3. Nbr1 thus contributes to specific steps in protein turnover regulation disrupted in several hereditary human diseases.
Mesh Terms:
Animals, Autophagy, Binding Sites, COS Cells, Cercopithecus aethiops, Endopeptidases, Endosomal Sorting Complexes Required for Transport, Humans, Ligands, Lysine, Mice, Microtubule-Associated Proteins, Polyubiquitin, Protein Binding, Protein Interaction Domains and Motifs, Proteins, Recombinant Fusion Proteins, Two-Hybrid System Techniques, Ubiquitin Thiolesterase
Animals, Autophagy, Binding Sites, COS Cells, Cercopithecus aethiops, Endopeptidases, Endosomal Sorting Complexes Required for Transport, Humans, Ligands, Lysine, Mice, Microtubule-Associated Proteins, Polyubiquitin, Protein Binding, Protein Interaction Domains and Motifs, Proteins, Recombinant Fusion Proteins, Two-Hybrid System Techniques, Ubiquitin Thiolesterase
FEBS Lett.
Date: Jun. 18, 2009
PubMed ID: 19427866
View in: Pubmed Google Scholar
Download Curated Data For This Publication
139351
Switch View:
- Interactions 10