scholarly journals Aberrant Activation of Atypical Protein Kinase C in Carbon Tetrachloride–Induced Oxidative Stress Provokes a Disturbance of Cell Polarity and Sealing of Bile Canalicular Lumen

2015 ◽  
Vol 185 (4) ◽  
pp. 958-968 ◽  
Author(s):  
Yosuke Horikoshi ◽  
Kanae Kitatani ◽  
Kentaro Toriumi ◽  
Nahoko Fukunishi ◽  
Yoshiko Itoh ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Kinase C ◽  
Carbon Tetrachloride ◽  
Protein Kinase ◽  
Cell Polarity ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C

The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42

2000 ◽  
Vol 2 (8) ◽  
pp. 531-539 ◽  
Author(s):  
Gérard Joberty ◽  
Clark Petersen ◽  
Lin Gao ◽  
Ian G. Macara
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Polarity ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C

scholarly journals Atypical protein kinase C controls sea urchin ciliogenesis

2011 ◽  
Vol 22 (12) ◽  
pp. 2042-2053 ◽  
Author(s):  
Gérard Prulière ◽  
Jacky Cosson ◽  
Sandra Chevalier ◽  
Christian Sardet ◽  
Janet Chenevert
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Polarity ◽  
Sea Urchin ◽  
Primary Cilium ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Motile Cilia ◽  
Sensory Processes

The atypical protein kinase C (aPKC) is part of the conserved aPKC/PAR6/PAR3 protein complex, which regulates many cell polarity events, including the formation of a primary cilium at the apical surface of epithelial cells. Cilia are highly organized, conserved, microtubule-based structures involved in motility, sensory processes, signaling, and cell polarity. We examined the distribution and function of aPKC in the sea urchin embryo, which forms a swimming blastula covered with motile cilia. We found that in the early embryo aPKC is uniformly cortical and becomes excluded from the vegetal pole during unequal cleavages at the 8- to 64-cell stages. During the blastula and gastrula stages the kinase localizes at the base of cilia, forming a ring at the transition zone between the basal body and the elongating axoneme. A dose-dependent and reversible inhibition of aPKC results in mislocalization of the kinase, defective ciliogenesis, and lack of swimming. Thus, as in the primary cilium of differentiated mammalian cells, aPKC controls the growth of motile cilia in invertebrate embryos. We suggest that aPKC might function to phosphorylate kinesin and so activate the transport of intraflagellar vesicles.

scholarly journals Neph-Nephrin Proteins Bind the Par3-Par6-Atypical Protein Kinase C (aPKC) Complex to Regulate Podocyte Cell Polarity

2008 ◽  
Vol 283 (34) ◽  
pp. 23033-23038 ◽  
Author(s):  
Björn Hartleben ◽  
Heiko Schweizer ◽  
Pauline Lübben ◽  
Malte P. Bartram ◽  
Clemens C. Möller ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Polarity ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C
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