The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors.
J Biol Chem
; 272(32): 19884-90, 1997 Aug 08.
Article
em En
| MEDLINE
| ID: mdl-9242653
ABSTRACT
The two known mannose 6-phosphate receptors (MPR46 and MPR300) both mediate the transport of Man-6-P-containing lysosomal proteins to lysosomes. However, the MPRs cannot be detected in lysosomes, instead they recycle between the plasma membrane and endosomes and between endosomes and the trans-Golgi network. Both, endocytosis from the plasma membrane and budding of transport vesicles from the trans-Golgi network involves the interaction of the receptor with the clathrin-coated vesicles-associated protein complexes AP1 and AP2. We have analyzed this interaction between the Golgi-restricted AP1 complex and the plasma membrane-restricted AP2 complex with the MPR46 tail in vitro by using a biosensor. AP1 and AP2 both bind to and dissociate from the MPR46 tail with similar kinetics. Using synthetic peptides corresponding to different MPR receptor tail regions in inhibition and binding studies, a common high affinity binding site for AP1 and AP2 and two separate high affinity binding sites for AP1 and AP2, respectively, were identified.
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Base de dados:
MEDLINE
Assunto principal:
Receptor IGF Tipo 2
/
Proteínas de Membrana
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article