Binding to PKC-3, but not to PAR-3 or to a conventional PDZ domain ligand, is required for PAR-6 function in C. elegans.
Dev Biol
; 340(1): 88-98, 2010 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-20122916
ABSTRACT
PAR-6 is a conserved protein important for establishment and maintenance of cell polarity in a variety of metazoans. PAR-6 proteins function together with PAR-3, aPKC and CDC-42. Mechanistic details of their interactions, however, are not fully understood. We studied the biochemical interactions between C. elegans PAR-6 and its binding partners and tested the requirements of these interactions in living worms. We show that PB1 domain-mediated binding of PAR-6 to PKC-3 is necessary for polarity establishment and PAR-6 cortical localization in C. elegans embryos. We also show that binding of PAR-6 and PAR-3 is mediated in vitro by a novel type of PDZ-PDZ interaction; the betaC strand of PAR-6 PDZ binds the betaD strand of PAR-3 PDZ1. However, this interaction is dispensable in vivo for PAR-6 function throughout the life of C. elegans. Mutations that specifically abolish conventional ligand binding to the PAR-6 PDZ domain also failed to affect PAR-6 function in vivo. We conclude that PAR-6 binding to PKC-3, but not to PAR-3 nor to a conventional PDZ ligand, is required for PAR-6 cortical localization and function in C. elegans.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteína Quinase C
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Caenorhabditis elegans
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Proteínas de Caenorhabditis elegans
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Domínios PDZ
Limite:
Animals
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article