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.
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ジャーナル |
Dev Biol
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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
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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
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リソース情報 |
線虫 |
tm1425 |