title: Centriole duplication: when PLK4 meets Ana2/STIL.
abstract: Polo-like kinase 4 is known to drive centriole duplication, but the relevant substrate remains elusive. A new study shows that PLK4 phosphorylates a key centriolar component, Ana2/STIL, to initiate centriole assembly.
authors.affiliation: Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Weill Cornell Graduate School of Medical Sciences, Cornell University, New York, NY 10065, USA.
authors.forename: Minhee
authors.initials: M
authors.lastname: Kim
authors.affiliation: Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
authors.forename: Chii Shyang
authors.initials: CS
authors.lastname: Fong
authors.affiliation: Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Weill Cornell Graduate School of Medical Sciences, Cornell University, New York, NY 10065, USA. Electronic address: tsoum@mskcc.org.
authors.forename: Meng-Fu Bryan
authors.initials: MF
authors.lastname: Tsou
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002502:Centrioles / Q000378:metabolism*; D004330:Drosophila / Q000378:metabolism*; D029721:Drosophila Proteins / Q000378:metabolism* / Q000502:physiology*; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000502:physiology*
chemical_list: D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; D008869:Microtubule-Associated Proteins; D017346:Protein Serine-Threonine Kinases