Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch.
Science
; 345(6195): 459-63, 2014 Jul 25.
Article
em En
| MEDLINE
| ID: mdl-25061211
ABSTRACT
Clathrin-mediated endocytosis (CME) is vital for the internalization of most cell-surface proteins. In CME, plasma membrane-binding clathrin adaptors recruit and polymerize clathrin to form clathrin-coated pits into which cargo is sorted. Assembly polypeptide 2 (AP2) is the most abundant adaptor and is pivotal to CME. Here, we determined a structure of AP2 that includes the clathrin-binding ß2 hinge and developed an AP2-dependent budding assay. Our findings suggest that an autoinhibitory mechanism prevents clathrin recruitment by cytosolic AP2. A large-scale conformational change driven by the plasma membrane phosphoinositide phosphatidylinositol 4,5-bisphosphate and cargo relieves this autoinhibition, triggering clathrin recruitment and hence clathrin-coated bud formation. This molecular switching mechanism can couple AP2's membrane recruitment to its key functions of cargo and clathrin binding.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Membrana Celular
/
Clatrina
/
Complexo 2 de Proteínas Adaptadoras
/
Subunidades beta do Complexo de Proteínas Adaptadoras
/
Polimerização
Limite:
Humans
Idioma:
En
Revista:
Science
Ano de publicação:
2014
Tipo de documento:
Article