Drosophila CK2 regulates lateral-inhibition during eye and bristle development.
Lateral inhibition is critical for cell fate determination and involves the functions of Notch (N) and its effectors, the Enhancer of Split Complex, E(spl)C repressors. Although E(spl) proteins mediate the repressive effects of N in diverse contexts, the role of phosphorylation was unclear. The studies we describe implicate a common role for the highly conserved Ser/Thr protein kinase CK2 during eye and bristle development. Compromising the functions of the catalytic (alpha) subunit of CK2 elicits a rough eye and defects in the interommatidial bristles (IOBs). These phenotypes are exacerbated by mutations in CK2 and suppressed by an increase in the dosage of this protein kinase. The appearance of the rough eye correlates, in time and space, to the specification and refinement of the 'founding' R8 photoreceptor. Consistent with this observation, compromising CK2 elicits supernumerary R8's at the posterior margin of the morphogenetic furrow (MF), a phenotype characteristic of loss of E(spl)C and impaired lateral inhibition. We also show that compromising CK2 elicits ectopic and split bristles. The former reflects the specification of excess bristle SOPs, while the latter suggests roles during asymmetric divisions that drive morphogenesis of this sensory organ. In addition, these phenotypes are exacerbated by mutations in CK2 or E(spl), indicating genetic interactions between these two loci. Given the centrality of E(spl) to the repressive effects of N, our studies suggest conserved roles for this protein kinase during lateral inhibition. Candidates for this regulation are the E(spl) repressors, the terminal effectors of this pathway.
Bose
Anasua
A
Department of Biology, Life Sciences Building, 53 Campus Drive, West Virginia University Morgantown, WV 26506, USA.
Kahali
Bhaskar
B
Zhang
Sophia
S
Lin
Jui-Ming
JM
Allada
Ravi
R
Karandikar
Umesh
U
Bidwai
Ashok P
AP
D000595:Amino Acid Sequence; D000818:Animals; D051792:Basic Helix-Loop-Helix Proteins / Q000235:genetics / Q000502:physiology; D019521:Body Patterning; D047390:Casein Kinase II / Q000235:genetics / Q000502:physiology*; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development*; D029721:Drosophila Proteins / Q000235:genetics / Q000502:physiology*; D005123:Eye / Q000254:growth & development; D017344:Genes, Insect; D010766:Phosphorylation; D034622:RNA Interference; D051880:Receptors, Notch / Q000235:genetics / Q000502:physiology; D012097:Repressor Proteins / Q000235:genetics / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D019892:eIF-2 Kinase / Q000235:genetics / Q000502:physiology
D051792:Basic Helix-Loop-Helix Proteins; D047390:Casein Kinase II; D029721:Drosophila Proteins; D051880:Receptors, Notch; D012097:Repressor Proteins; D019892:eIF-2 Kinase; C121960:E(spl)m7-HLH protein, Drosophila; C497759:N protein, Drosophila