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

Autor: Elisabeth Knust, Andreas Wodarz, Alexandra Grimm, Andreas Ramrath
Rok vydání: 2000
Předmět:
Embryo
Nonmammalian
572.8
tight junction
Genes
Insect
0302 clinical medicine
Bazooka
Cell polarity
Drosophila Proteins
In Situ Hybridization
Protein Kinase C
Neurons
0303 health sciences
Stem Cells
Apical cortex
Intracellular Signaling Peptides and Proteins
Cell Polarity
Gene Expression Regulation
Developmental
Cell biology
atypical PKC
Original Article
Drosophila
Cell Division
Drosophila Protein
Protein Binding
573.8
Gene isoform
animal structures
612.8
Molecular Sequence Data
Biology
Cell fate determination
asymmetric cell division
Gene Expression Regulation
Enzymologic
Tight Junctions
03 medical and health sciences
Neuroblast
Animals
RNA
Messenger
Protein kinase C
030304 developmental biology
Sequence Homology
Amino Acid
Epithelial Cells
Cell Biology
Spindle apparatus
Mutagenesis
Carrier Proteins
cell polarity
030217 neurology & neurosurgery
Zdroj: The Journal of Cell Biology
ISSN: 1540-8140
0021-9525
DOI: 10.1083/jcb.150.6.1361
Popis: 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.
Databáze: OpenAIRE
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