Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting.

Developmental cell | Jun 4, 2007

http://www.ncbi.nlm.nih.gov/pubmed/17543868

The yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex deliver ubiquitinated transmembrane proteins to the ESCRT endosomal-sorting pathway. The Vps27/Hse1 complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. We have solved the crystal structure of the core responsible for the assembly of the Vps27/Hse1 complex at 3.0 A resolution. The structure consists of two intertwined GAT domains, each consisting of two helices from one subunit and one from the other. The two GAT domains are connected by an antiparallel coiled coil, forming a 90 A-long barbell-like structure. This structure places the domains of Vps27 and Hse1 that recruit ubiquitinated cargo and deubiquitinating enzymes close to each other. Coarse-grained Monte Carlo simulations of the Vps27/Hse1 complex on a membrane show how the complex binds cooperatively to lipids and ubiquitinated membrane proteins and acts as a scaffold for ubiquitination reactions.

Pubmed ID: 17543868 RIS Download

Mesh terms: Amino Acid Sequence | Chromatography, Gel | Crystallography, X-Ray | Endosomal Sorting Complexes Required for Transport | Immunoprecipitation | Models, Molecular | Molecular Sequence Data | Mutagenesis, Site-Directed | Mutation | Protein Binding | Protein Structure, Tertiary | Protein Transport | Receptors, Cytoplasmic and Nuclear | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Sequence Homology, Amino Acid | Ubiquitin | Vesicular Transport Proteins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: Intramural NIH HHS, Id: Z01 DK036118-14
  • Agency: Intramural NIH HHS, Id: Z01 DK036126-01

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.