Document Detail

Location of auxilin within a clathrin cage.
MedLine Citation:
PMID:  14757058     Owner:  NLM     Status:  MEDLINE    
The Dna J homologue, auxilin, acts as a co-chaperone for Hsc70 in the uncoating of clathrin-coated vesicles during endocytosis. Biochemical studies have aided understanding of the uncoating mechanism but until now there was no structural information on how auxilin interacts with the clathrin cage. Here we have determined the three-dimensional structure of a complex of auxilin with clathrin cages by cryo-electron microscopy and single particle analysis. We show that auxilin forms a discrete shell of density on the inside of the clathrin cage. Peptide competition assays confirm that a candidate clathrin box motif in auxilin, LLGLE, can bind to a clathrin construct containing the beta-propeller domain and also displace the well-characterised LLNLD clathrin box motif derived from the beta-adaptin hinge region. The means by which auxilin could both aid clathrin coat assembly and displace clathrin from AP2 during uncoating is discussed.
Corinne J Smith; Timothy R Dafforn; Helen Kent; Catherine A Sims; Kavita Khubchandani-Aswani; Lin Zhang; Helen R Saibil; Barbara M F Pearse
Related Documents :
16453478 - Point mutation in the 30-k open reading frame of tmv implicated in temperature-sensitiv...
18573978 - Self-assembling peptides: from bio-inspired materials to bone regeneration.
19344168 - Characterization and bacterial response of zinc oxide particles prepared by a biominera...
20409488 - Assembly pathway of a designed alpha-helical protein fiber.
10383478 - Secost: sequence-conformation-structure database for amino acid residues in proteins.
21110718 - Biochemical and immunohistochemical analyses of gnrh-like peptides in the nerve ganglio...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  336     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2004 Feb 
Date Detail:
Created Date:  2004-02-03     Completed Date:  2004-03-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  461-71     Citation Subset:  IM    
Department of Crystallography, Birkbeck College, Malet Street, WC1E 7HX, England, London, UK.
Data Bank Information
Bank Name/Acc. No.:
SWISSPROT/Q05140;  Q27974
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Motifs
Amino Acid Sequence
Auxilins / chemistry,  metabolism*,  ultrastructure*
Binding Sites
Brain / metabolism
Clathrin / chemistry*,  metabolism,  ultrastructure*
Cryoelectron Microscopy
Fluorescence Polarization
Models, Molecular
Molecular Sequence Data
PTEN Phosphohydrolase
Phosphoric Monoester Hydrolases / chemistry
Protein Binding
Protein Conformation
Tumor Suppressor Proteins / chemistry
Reg. No./Substance:
0/Auxilins; 0/Clathrin; 0/Tumor Suppressor Proteins; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC Phosphohydrolase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Recognition and separation of single particles with size variation by statistical analysis of their ...
Next Document:  Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalyti...