Members of the mammalian protein kinase C (PKC) superfamily play key regulatory roles in a multitude of cellular processes, ranging from control of fundamental cell autonomous activities, such as proliferation, to more organismal functions, such as memory. However, understanding of mammalian PKC signalling systems is complicated by the large number of family members. Significant progress has been made through studies based on comparative analysis, which have defined a number of regulatory elements in PKCs which confer specific location and activation signals to each isotype. Further studies on simple organisms have shown that PKC signalling paradigms are conserved through evolution from yeast to humans, underscoring the importance of this family in cellular signalling and giving novel insights into PKC function in complex mammalian systems.

/pdf/the-extended-protein-kinase-c-superfamily-123ce50z7t.pdf

The extended protein kinase C superfamily.

Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic motif. This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.

/pdf/regulation-of-the-abc-kinases-by-phosphorylation-protein-m2lho8can2.pdf

Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm.

The establishment and maintenance of polarity is of fundamental importance for the function of epithelial and neuronal cells. In Drosophila, the multi-PDZ domain protein Bazooka (Baz) is required for establishment of apico-basal polarity in epithelia and in neuroblasts, the stem cells of the central nervous system. In the latter, Baz anchors Inscuteable in the apical cytocortex, which is essential for asymmetric localization of cell fate determinants and for proper orientation of the mitotic spindle. Here we show that Baz directly binds to the Drosophila atypical isoform of protein kinase C and that both proteins are mutually dependent on each other for correct apical localization. Loss-of-function mutants of the Drosophila atypical isoform of PKC show loss of apico-basal polarity, multilayering of epithelia, mislocalization of Inscuteable and abnormal spindle orientation in neuroblasts. Together, these data provide strong evidence for the existence of an evolutionary conserved mechanism that controls apico-basal polarity in epithelia and neuronal stem cells. This study is the first functional analysis of an atypical protein kinase C isoform using a loss-of-function allele in a genetically tractable organism.

https://rupress.org/jcb/article-pdf/150/6/1361/1292983/0006042.pdf

Drosophila Atypical Protein Kinase C Associates with Bazooka and Controls Polarity of Epithelia and Neuroblasts

The intestine is one of the major organs in C. elegans and is largely responsible for food digestion and assimilation as well as the synthesis and storage of macromolecules. In addition, the intestine is emerging as a powerful experimental system in which to study such universal biological phenomena as vesicular trafficking, biochemical clocks, stress responses and aging. The present chapter describes some of these many and varied properties of the C. elegans intestine: the embryonic cell lineage, intestine morphogenesis, structure and physiology of the intestinal cell and, finally, the transcription factor network controlling intestine development and function.

/pdf/the-c-elegans-intestine-31ioljciku.pdf

The C. elegans intestine.

http://worms.zoology.wisc.edu/pdfs/leung-DB.pdf

Organogenesis of the Caenorhabditis elegans intestine.

Structure, Expression, and Properties of an Atypical Protein Kinase C (PKC3) from Caenorhabditis elegans: PKC3 IS REQUIRED FOR THE NORMAL PROGRESSION OF EMBRYOGENESIS AND VIABILITY OF THE ORGANISM *

Characterization of a Novel Protein Kinase D: CAENORHABDITIS ELEGANS DKF-1 IS ACTIVATED BY TRANSLOCATION-PHOSPHORYLATION AND REGULATES MOVEMENT AND GROWTH IN VIVO

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Structure, Expression, and Properties of an Atypical Protein Kinase C (PKC3) from Caenorhabditis elegans: PKC3 IS REQUIRED FOR THE NORMAL PROGRESSION OF EMBRYOGENESIS AND VIABILITY OF THE ORGANISM *

Characterization of a Novel Protein Kinase D: CAENORHABDITIS ELEGANS DKF-1 IS ACTIVATED BY TRANSLOCATION-PHOSPHORYLATION AND REGULATES MOVEMENT AND GROWTH IN VIVO