MersV1, Main, Exploration, bibRecord, 004069

Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs

Identifieur interne : 004069 ( Main/Exploration ); précédent : 004068; suivant : 004070

Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs

Auteurs : Shu-Hui Liu [États-Unis] ; Mei Lie Wong [États-Unis] ; Charles S. Craik [États-Unis] ; Frances M. Brodsky [États-Unis]

Source :

Cell [ 0092-8674 ] ; 1995.

RBID : ISTEX:88AF3341FD0CDD2F45F5B4B176A881DDE5271C3B

English descriptors

Teeft :
- Adaptor, Adaptor molecules, Affinity resin, Antibody binding, Bacterial lysate, Binding buffer, Binding sites, Biol, Bovine, Bovine brain clathrin, Bovine clathrin, Brodsky, Cdna, Cell biol, Chain sequence, Clathrin, Clathrin assembly, Clathrin lattice, Clathrin light chains, Clathrin triskelion, Clathrin triskelions, Coexpressed, Deletion, Deletion mutagenesis, Electron microscopy, Fragment, Fragments coexpressed, Fusion proteins, Heavy chain, Heavy chain fragment, Kirchhausen, Lattice, Light chain, Light chain binding, Light chains, Light region, Light sites, Lysate, Marker proteins, Mutant, Nathke, Parham, Peak fraction, Previous studies, Recombinant, Recombinant proteins, Residue, Size exclusion chromatography, Trimer, Trimerization, Trimerization domain, Triskelion, Triskelion vertex, Ungewickell, Uranyl acetate, Vesicle, Whole triskelion.

Abstract

Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.

Url:

https://api.istex.fr/ark:/67375/6H6-3KJ6BST1-F/fulltext.pdf

DOI: 10.1016/0092-8674(95)90167-1

Affiliations:

États-Unis

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Le document en format XML

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<term>Bacterial lysate</term>
<term>Binding buffer</term>
<term>Binding sites</term>
<term>Biol</term>
<term>Bovine</term>
<term>Bovine brain clathrin</term>
<term>Bovine clathrin</term>
<term>Brodsky</term>
<term>Cdna</term>
<term>Cell biol</term>
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<front><div type="abstract" xml:lang="en">Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.</div>
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Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs

Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri