RRC ID 29123
著者 Li J, Kim H, Aceto DG, Hung J, Aono S, Kemphues KJ.
タイトル 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.
ジャーナル Dev Biol
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.
巻・号 340(1)
ページ 88-98
公開日 2010-4-1
DOI 10.1016/j.ydbio.2010.01.023
PII S0012-1606(10)00052-7
PMID 20122916
PMC PMC2834849
MeSH Animals Animals, Genetically Modified Caenorhabditis elegans / metabolism* Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Caenorhabditis elegans Proteins / physiology* Embryo, Nonmammalian / metabolism Fluorescent Antibody Technique Ligands PDZ Domains* Protein Kinase C / genetics Protein Kinase C / metabolism* Protein Serine-Threonine Kinases
IF 2.896
引用数 23
WOS 分野 DEVELOPMENTAL BIOLOGY
リソース情報
線虫 tm1425