A kinase gets caspases into shape.
Two new papers (Kuranaga et al., 2006; Oshima et al., 2006) describe a previously uncharacterized Drosophila kinase (DmIKK epsilon) that regulates the abundance of DIAP1, a protein best known for its ability to inhibit apoptosis. However, DmIKK epsilon-mediated degradation of DIAP1 does not regulate apoptosis as might be predicted but instead regulates actin dynamics, cell morphology, and the differentiation of sensory organ precursor cells.
Montell
Denise J
DJ
Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205, USA. dmontell@jhmi.edu
D008841:Actin Cytoskeleton / Q000378:metabolism; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000378:metabolism*; D002454:Cell Differentiation / Q000235:genetics*; D048430:Cell Shape / Q000502:physiology; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D051034:Inhibitor of Apoptosis Proteins / Q000378:metabolism*; D010770:Phosphotransferases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D012679:Sense Organs / Q000166:cytology / Q000196:embryology* / Q000378:metabolism
C111891:DIAP1 protein, Drosophila; D029721:Drosophila Proteins; D051034:Inhibitor of Apoptosis Proteins; D010770:Phosphotransferases; D020169:Caspases; C118731:dronc protein, Drosophila