Interaction between Sec7p and Pik1p: the first clue for the regulation of a coincidence detection signal.
Eur J Cell Biol
; 89(8): 575-83, 2010 Aug.
Article
em En
| MEDLINE
| ID: mdl-20434792
ABSTRACT
Sec7p, a guanine nucleotide exchange factor, regulates the activation of small Arf GTPases, which function in the formation of distinct classes of transport carriers from the Golgi. The recruitment of a subset of Arf effectors depends on the cooperation between these GTPases and phosphatidylinositol 4-phosphate. Here, we show that the catalytic domain of Sec7p interacts with a conserved region of the Golgi phosphatidylinositol 4-kinase Pik1p. We found that Sec7p and Pik1p as well as its product, colocalize at the late Golgi. Gea1p/Gea2p, an alternative pair of Arf activators, do not bind to Pik1p and function on a different Golgi sub-compartment. Sec7p and Pik1p interact with each other and cooperate in the formation of clathrin-coated vesicles. This interaction reveals a distinct role for Sec7p among the Golgi Arf-GEFs and provides a working model for the coordinated generation of Arf-GTP and phosphatiylinositol 4-phosphate as dual signal for specific recruitment of clathrin coats to the late Golgi.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
1-Fosfatidilinositol 4-Quinase
/
Fatores de Troca do Nucleotídeo Guanina
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Transporte Proteico
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Proteínas de Saccharomyces cerevisiae
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Complexo de Golgi
Tipo de estudo:
Diagnostic_studies
/
Prognostic_studies
Idioma:
En
Revista:
Eur J Cell Biol
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Alemanha