title: The CASK/Lin-2 Drosophila homologue, Camguk, could play a role in epithelial patterning and in neuronal targeting.
abstract: Drosophila Camguk (Cmg) is a member of the CAMGUK subfamily of the MAGUK family of proteins which are localized at cell junction and other plasma membrane specialized regions, from worms to mammals. The protein structure of Cmg, as the other CAMGUK proteins, is characterized by only one PDZ domain and an additional CaM kinase domain, similar to CaMKII. While the mammalian ortholog CASKs play an important role in synaptic protein targeting and in synaptic plasticity, the Drosophila Cmg role is unknown. To study its potential role, we reported a detailed analysis of mRNA distribution of the Drosophila cmg gene at cellular and developmental level, during embryonic, larval, pupal and adult stages. The transient cmg transcription in midgut and Malpighian tubules may suggest a potential function in cell junction formation and in epithelial tissue patterning. Interestingly, cmg transcription increases substantially during embryonic neuroblast proliferation, becoming predominant in the developing central nervous system (CNS) during embryonic and postembryonic development stages and in the mature brain. In addition, a high transcriptional level was detected in the eye imaginal discs and in the adult retina, demonstrating a specific and continuous expression of cmg in neuroblasts and photoreceptor neurons, from the onset of cytodifferentiation. Our findings suggest that Cmg could play a potential role in transmembrane protein targeting, particularly in synapses. These observations suggest the existence of a common highly conserved mechanism involved in forming and maintaining proper synaptic protein targeting, which are fundamental features of synaptic plasticity, learning and memory. Through its function, the CaM kinase domain-containing Cmg may be involved in signal transduction cascade. Its potential relation to Calmodulin and CaMKII is discussed.
authors: Faculté de Médecine Necker, UMR 8602 CNRS, 156 rue de Vaugirard, Paris, 75015, France.
authors: C
authors: C
authors: Lopes
authors: S
authors: S
authors: Gassanova
authors: J M
authors: JM
authors: Delabar
authors: M
authors: M
authors: Rachidi
mesh_terms: D000818:Animals; D019521:Body Patterning / Q000235:genetics; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000196:embryology / Q000235:genetics / Q000502:physiology*; D004625:Embryo, Nonmammalian / Q000502:physiology; D004847:Epithelial Cells / Q000166:cytology / Q000502:physiology; D018507:Gene Expression Regulation, Developmental; D017344:Genes, Insect; D051528:Guanylate Kinases; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism; D017403:In Situ Hybridization; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D009474:Neurons / Q000502:physiology*; D009703:Nucleoside-Phosphate Kinase / Q000235:genetics* / Q000378:metabolism*; D013569:Synapses / Q000502:physiology
chemical_list: D029721:Drosophila Proteins; D015801:Helminth Proteins; C097978:Lin-2 protein, C elegans; D008565:Membrane Proteins; C106868:CASK kinases; C099190:CASK protein, Drosophila; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D009703:Nucleoside-Phosphate Kinase; D051528:Guanylate Kinases