title: Interphase centrosome organization by the PLP-Cnn scaffold is required for centrosome function.
abstract: Pericentriolar material (PCM) mediates the microtubule (MT) nucleation and anchoring activity of centrosomes. A scaffold organized by Centrosomin (Cnn) serves to ensure proper PCM architecture and functional changes in centrosome activity with each cell cycle. Here, we investigate the mechanisms that spatially restrict and temporally coordinate centrosome scaffold formation. Focusing on the mitotic-to-interphase transition in Drosophila melanogaster embryos, we show that the elaboration of the interphase Cnn scaffold defines a major structural rearrangement of the centrosome. We identify an unprecedented role for Pericentrin-like protein (PLP), which localizes to the tips of extended Cnn flares, to maintain robust interphase centrosome activity and promote the formation of interphase MT asters required for normal nuclear spacing, centrosome segregation, and compartmentalization of the syncytial embryo. Our data reveal that Cnn and PLP directly interact at two defined sites to coordinate the cell cycle-dependent rearrangement and scaffolding activity of the centrosome to permit normal centrosome organization, cell division, and embryonic viability.
authors.affiliation: Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Dorothy A
authors.initials: DA
authors.lastname: Lerit
authors.affiliation: Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Holly A
authors.initials: HA
authors.lastname: Jordan
authors.affiliation: Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
authors.forename: John S
authors.initials: JS
authors.lastname: Poulton
authors.affiliation: Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Carey J
authors.initials: CJ
authors.lastname: Fagerstrom
authors.affiliation: Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Galletta
authors.affiliation: Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
authors.forename: Mark
authors.initials: M
authors.lastname: Peifer
authors.affiliation: Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 Nasser@nih.gov.
authors.forename: Nasser M
authors.initials: NM
authors.lastname: Rusan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002148:Calmodulin-Binding Proteins; D018385:Centrosome / Q000378:metabolism*; D020090:Chromosome Segregation; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000378:metabolism; D042822:Genomic Instability; D018398:Homeodomain Proteins / Q000378:metabolism*; D007399:Interphase; D008870:Microtubules / Q000378:metabolism; D008938:Mitosis; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D021381:Protein Transport
chemical_list: D002148:Calmodulin-Binding Proteins; D029721:Drosophila Proteins; D018398:Homeodomain Proteins; C483309:Plp protein, Drosophila; C098130:cnn protein, Drosophila