Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans.
Asymmetric cell divisions, critically important to specify cell types in the development of multicellular organisms, require polarized distribution of cytoplasmic components and the proper alignment of the mitotic apparatus. In Caenorhabditis elegans, the maternally expressed protein, PAR-3, is localized to one pole of asymmetrically dividing blastomeres and is required for these asymmetric divisions. In this paper, we report that an atypical protein kinase C (PKC-3) is essential for proper asymmetric cell divisions and co-localizes with PAR-3. Embryos depleted of PKC-3 by RNA interference die showing Par-like phenotypes including defects in early asymmetric divisions and mislocalized germline-specific granules (P granules). The defective phenotypes of PKC-3-depleted embryos are similar to those exhibited by mutants for par-3 and another par gene, par-6. Direct interaction of PKC-3 with PAR-3 is shown by in vitro binding analysis. This result is reinforced by the observation that PKC-3 and PAR-3 co-localize in vivo. Furthermore, PKC-3 and PAR-3 show mutual dependence on each other and on three of the other par genes for their localization. We conclude that PKC-3 plays an indispensable role in establishing embryonic polarity through interaction with PAR-3.
Fundamental Research Laboratories, NEC Corporation, Tsukuba, Ibaraki 305, Japan. ytabuse@frl.cl.nec.co.jp
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Y
Tabuse
Y
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Izumi
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Piano
K J
KJ
Kemphues
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Miwa
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Ohno
D000818:Animals; D017173:Caenorhabditis elegans / Q000187:drug effects / Q000196:embryology* / Q000201:enzymology* / Q000235:genetics; D029742:Caenorhabditis elegans Proteins; D002118:Calcium / Q000378:metabolism; D016764:Cell Polarity / Q000235:genetics*; D018509:DNA, Helminth / Q000737:chemistry; D004075:Diglycerides / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000187:drug effects / Q000201:enzymology; D004789:Enzyme Activation; D018507:Gene Expression Regulation, Developmental; D017238:Genes, Helminth; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016376:Oligonucleotides, Antisense / Q000494:pharmacology; D010718:Phosphatidylserines / Q000378:metabolism; D011485:Protein Binding; D011493:Protein Kinase C / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D018510:RNA, Helminth / Q000494:pharmacology
D029742:Caenorhabditis elegans Proteins; D018509:DNA, Helminth; D004075:Diglycerides; D015801:Helminth Proteins; D016376:Oligonucleotides, Antisense; D010718:Phosphatidylserines; D018510:RNA, Helminth; C097238:PAR-3 protein, C elegans; D017346:Protein Serine-Threonine Kinases; C115015:PKC-3 protein; D011493:Protein Kinase C; D002118:Calcium