Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells.
Traffic
; 1(6): 494-503, 2000 Jun.
Article
en En
| MEDLINE
| ID: mdl-11208135
In epithelial cells, endocytosed transferrin and its receptor, which cycle basolaterally, have been shown to transit through recycling endosomes which can also be accessed by markers internalized from the apical surface. In this work, we have used an in vitro assay to follow transfer of an endocytosed marker from apical or basolateral early endosomes to recycling endosomes labeled with transferrin. We show that calmodulin (CaM) function is necessary for transfer and identified myr4, a member of the unconventional myosin superfamily known to use CaM as a light chain, as a possible target protein for CaM. Since myr4 is believed to act as an actin-based mechanoenzyme, we tested the role of polymerized actin in the assay. Our data show that conditions which either prevent actin polymerization or induce the breakdown of existing filaments strongly inhibit interactions between recycling endosomes and either set of early endosomes. Altogether, our data indicate that trafficking at early steps of the endocytic pathway in Madin-Darby Canine Kidney cells depends on the actin-based mechanoenzyme myr4, its light chain CaM, and polymerized actin.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Endosomas
/
Calmodulina
/
Miosinas
/
Miosina Tipo I
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Traffic
Asunto de la revista:
FISIOLOGIA
Año:
2000
Tipo del documento:
Article
País de afiliación:
Austria
Pais de publicación:
Reino Unido