title: The coronin-like protein POD-1 is required for anterior-posterior axis formation and cellular architecture in the nematode caenorhabditis elegans.
abstract: Establishment of anterior-posterior (a-p) polarity in the Caenorhabditis elegans embryo depends on filamentous (F-) actin. Previously, we isolated an F-actin-binding protein that was enriched in the anterior cortex of the one-cell embryo and was hypothesized to link developmental polarity to the actin cytoskeleton. Here, we identify this protein, POD-1, as a new member of the coronin family of actin-binding proteins. We have generated a deletion within the pod-1 gene. Elimination of POD-1 from early embryos results in a loss of physical and molecular asymmetries along the a-p axis. For example, PAR-1 and PAR-3, which themselves are polarized and required for a-p polarity, are delocalized in pod-1 mutant embryos. However, unlike loss of PAR proteins, loss of POD-1 gives rise to the formation of abnormal cellular structures, namely large vesicles of endocytic origin, membrane protrusions, unstable cell divisions, a defective eggshell, and deposition of extracellular material. We conclude that, analogous to coronin, POD-1 plays an important role in intracellular trafficking and organizing specific aspects of the actin cytoskeleton. We propose models to explain how the role of POD-1 in basic cellular processes could be linked to the generation of polarity along the embryonic a-p axis.
authors.affiliation: Department of Biology, The University of California, San Diego, La Jolla, California 92093, USA.
authors.forename: C A
authors.initials: CA
authors.lastname: Rappleye
authors.forename: A R
authors.initials: AR
authors.lastname: Paredez
authors.forename: C W
authors.initials: CW
authors.lastname: Smith
authors.forename: K L
authors.initials: KL
authors.lastname: McDonald
authors.forename: R V
authors.initials: RV
authors.lastname: Aroian
mesh_terms: D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D019521:Body Patterning / Q000502:physiology*; D017173:Caenorhabditis elegans / Q000196:embryology* / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure; D029742:Caenorhabditis elegans Proteins; D002453:Cell Cycle; D005109:Extracellular Matrix; D005456:Fluorescent Dyes / Q000378:metabolism; D017238:Genes, Helminth; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D007211:Indoles / Q000378:metabolism; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D009997:Osmotic Pressure; D010539:Permeability; D017346:Protein Serine-Threonine Kinases; D011726:Pyridinium Compounds / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism
chemical_list: D000199:Actins; D029742:Caenorhabditis elegans Proteins; C092350:FM 4-64; D005456:Fluorescent Dyes; D015801:Helminth Proteins; D007211:Indoles; D008840:Microfilament Proteins; C401782:POD-1 protein, C elegans; D011726:Pyridinium Compounds; D000644:Quaternary Ammonium Compounds; C072061:coronin proteins; C007293:DAPI; C097238:PAR-3 protein, C elegans; D017346:Protein Serine-Threonine Kinases