title: Planar cell polarity acts through septins to control collective cell movement and ciliogenesis.
abstract: The planar cell polarity (PCP) signaling pathway governs collective cell movements during vertebrate embryogenesis, and certain PCP proteins are also implicated in the assembly of cilia. The septins are cytoskeletal proteins controlling behaviors such as cell division and migration. Here, we identified control of septin localization by the PCP protein Fritz as a crucial control point for both collective cell movement and ciliogenesis in Xenopus embryos. We also linked mutations in human Fritz to Bardet-Biedl and Meckel-Gruber syndromes, a notable link given that other genes mutated in these syndromes also influence collective cell movement and ciliogenesis. These findings shed light on the mechanisms by which fundamental cellular machinery, such as the cytoskeleton, is regulated during embryonic development and human disease.
authors.affiliation: Section of Molecular Cell and Developmental Biology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Su Kyoung
authors.initials: SK
authors.lastname: Kim
authors.forename: Asako
authors.initials: A
authors.lastname: Shindo
authors.forename: Tae Joo
authors.initials: TJ
authors.lastname: Park
authors.forename: Edwin C
authors.initials: EC
authors.lastname: Oh
authors.forename: Srimoyee
authors.initials: S
authors.lastname: Ghosh
authors.forename: Ryan S
authors.initials: RS
authors.lastname: Gray
authors.forename: Richard A
authors.initials: RA
authors.lastname: Lewis
authors.forename: Colin A
authors.initials: CA
authors.lastname: Johnson
authors.forename: Tania
authors.initials: T
authors.lastname: Attie-Bittach
authors.forename: Nicholas
authors.initials: N
authors.lastname: Katsanis
authors.forename: John B
authors.initials: JB
authors.lastname: Wallingford
mesh_terms: D000015:Abnormalities, Multiple / Q000235:genetics; D000818:Animals; D020788:Bardet-Biedl Syndrome / Q000235:genetics*; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D002465:Cell Movement; D016764:Cell Polarity; D048430:Cell Shape; D002923:Cilia / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000502:physiology; D047108:Embryonic Development; D005260:Female; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D005775:Gastrula / Q000166:cytology; D056726:Genetic Association Studies; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D053823:Hedgehog Proteins / Q000378:metabolism; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D009024:Morphogenesis; D050505:Mutant Proteins / Q000378:metabolism; D009154:Mutation; D058112:Septins; D013577:Syndrome; D029867:Xenopus Proteins / Q000235:genetics / Q000378:metabolism*; D014982:Xenopus laevis; D000099274:Frizzled-Related Proteins
chemical_list: D003598:Cytoskeletal Proteins; D019204:GTP-Binding Proteins; D006023:Glycoproteins; D053823:Hedgehog Proteins; D047908:Intracellular Signaling Peptides and Proteins; D050505:Mutant Proteins; D058112:Septins; D029867:Xenopus Proteins; D000099274:Frizzled-Related Proteins; C552239:sept2 protein, Xenopus; C552238:sept7 protein, Xenopus