AP-1 in Toxoplasma gondii mediates biogenesis of the rhoptry secretory organelle from a post-Golgi compartment.
J Biol Chem
; 278(7): 5343-52, 2003 Feb 14.
Article
em En
| MEDLINE
| ID: mdl-12446678
ABSTRACT
We have previously demonstrated that Toxoplasma gondii has a tyrosine-based sorting system, which mediates protein targeting to the lysosome-like rhoptry secretory organelle. We now show that rhoptry protein targeting is also dependent on a dileucine motif and occurs from a post-Golgi endocytic organelle to mature rhoptries in an adaptin-dependent fashion. The T. gondii AP-1 adaptin complex is implicated in this transport because the micro1 chain of T. gondii AP-1 (a) was localized to multivesicular endosomes and the limiting and luminal membranes of the rhoptries; (b) bound to endocytic tyrosine motifs in rhoptry proteins, but not in proteins from dense granule secretory organelles; (c) when mutated in predicted tyrosine-binding motifs, led to accumulation of the rhoptry protein ROP2 in a post-Golgi multivesicular compartment; and (d) when depleted via antisense mRNA, resulted in accumulation of multivesicular endosomes and immature rhoptries. These are the first results to implicate AP-1 in transport from a post-Golgi compartment to a mature secretory organelle and substantially expand the role for AP-1 in anterograde protein transport.
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Base de dados:
MEDLINE
Assunto principal:
Toxoplasma
/
Proteínas de Protozoários
/
Vesículas Secretórias
/
Complexo 1 de Proteínas Adaptadoras
/
Proteínas de Membrana
Limite:
Animals
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article