Crn7 interacts with AP-1 and is required for the maintenance of Golgi morphology and protein export from the Golgi.
J Biol Chem
; 281(41): 31070-8, 2006 Oct 13.
Article
em En
| MEDLINE
| ID: mdl-16905771
ABSTRACT
Crn7 is a novel cytosolic mammalian WD-repeat protein of unknown function that associates with Golgi membranes. Here, we demonstrate that Crn7 knockdown by small interfering RNA results in dramatic changes in the Golgi morphology and function. First, the Golgi ribbon is disorganized in Crn7 KD cells. Second, the Golgi export of several marker proteins including VSV envelope G glycoprotein is greatly reduced but not the retrograde protein import into the Golgi complex. We further establish that Crn7 co-precipitates with clathrin adaptor AP-1 but is not required for AP-1 targeting to Golgi membranes. We identify tyrosine 288-based motif as part of a canonical YXXPhi sorting signal and a major mu1-adaptin binding site in vitro. This study provides the first insight into the function of mammalian Crn7 protein in the Golgi complex.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fator de Transcrição AP-1
/
Complexo de Golgi
/
Proteínas dos Microfilamentos
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2006
Tipo de documento:
Article