RRC ID 51453
著者 Rodriguez J, Peglion F, Martin J, Hubatsch L, Reich J, Hirani N, Gubieda AG, Roffey J, Fernandes AR, St Johnston D, Ahringer J, Goehring NW.
タイトル aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity.
ジャーナル Dev Cell
Abstract The conserved polarity effector proteins PAR-3, PAR-6, CDC-42, and atypical protein kinase C (aPKC) form a core unit of the PAR protein network, which plays a central role in polarizing a broad range of animal cell types. To functionally polarize cells, these proteins must activate aPKC within a spatially defined membrane domain on one side of the cell in response to symmetry-breaking cues. Using the Caenorhabditis elegans zygote as a model, we find that the localization and activation of aPKC involve distinct, specialized aPKC-containing assemblies: a PAR-3-dependent assembly that responds to polarity cues and promotes efficient segregation of aPKC toward the anterior but holds aPKC in an inactive state, and a CDC-42-dependent assembly in which aPKC is active but poorly segregated. Cycling of aPKC between these distinct functional assemblies, which appears to depend on aPKC activity, effectively links cue-sensing and effector roles within the PAR network to ensure robust establishment of polarity.
巻・号 42(4)
ページ 400-415.e9
公開日 2017-8-21
DOI 10.1016/j.devcel.2017.07.007
PII S1534-5807(17)30549-X
PMID 28781174
PMC PMC5563072
MeSH Animals Caenorhabditis elegans / embryology Caenorhabditis elegans / genetics Caenorhabditis elegans / metabolism Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Cell Cycle Proteins / genetics Cell Cycle Proteins / metabolism Cell Polarity* Cyclic AMP-Dependent Protein Kinases / genetics Cyclic AMP-Dependent Protein Kinases / metabolism* GTP-Binding Proteins / genetics GTP-Binding Proteins / metabolism HEK293 Cells Humans Protein Binding Protein Serine-Threonine Kinases / genetics Protein Serine-Threonine Kinases / metabolism* Zygote / metabolism
IF 10.092
引用数 51
リソース情報
線虫 tm2616