title: Chemoreceptor-mediated polymerization and depolymerization of actin in hair bundles of sea anemones.
abstract: Hair bundles located on tentacles of sea anemones are morphodynamic mechanoreceptors employed to regulate discharge of nematocysts into swimming prey. Activation of chemoreceptors for N-acetylated sugars is known to induce anemone hair bundles to elongate while shifting discharge to lower frequencies matching those produced by calmly swimming prey. In the continued presence of N-acetylated sugars, activation of proline receptors is known to induce hair bundles to shorten while shifting nematocyst discharge to higher frequencies presumed to correspond to movements produced by wounded, struggling prey. In the present study, N-acetylneuraminic acid (NANA) causes stereocilia to become more intensely fluorescent in confocal optical sections of phalloidin-stained specimens, suggesting that receptors for N-acetylated sugars initiate processes to increase the density of F-actin within stereocilia. Computer analysis of electron micrographs is consistent with this interpretation for large diameter stereocilia but not for small diameter stereocilia. In the continued presence of NANA, proline causes fluorescence intensity of phalloidin to decrease to or below control levels. DNaseI uniformly stains large diameter stereocilia, suggesting that these stereocilia contain a pool of G-actin. Fluorescence intensity of DNaseI in stereocilia is significantly less bright in specimens exposed to NANA alone than in specimens exposed to proline in the continued presence of NANA. It appears that whereas activated receptors for NANA induce G-actin to polymerize in large diameter stereocilia, activated receptors for proline induce F-actin to depolymerize, restoring G-actin pools.
authors.affiliation: Department of Biology, University of Southwestern Louisiana, Lafayette 70504-2451, USA.
authors.forename: G M
authors.initials: GM
authors.lastname: Watson
authors.forename: J
authors.initials: J
authors.lastname: Roberts
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D002628:Chemoreceptor Cells / Q000502:physiology*; D002923:Cilia / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure; D003850:Deoxyribonuclease I / Q000187:drug effects; D008465:Mechanoreceptors / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D019158:N-Acetylneuraminic Acid; D010590:Phalloidine; D011108:Polymers / Q000378:metabolism; D011392:Proline / Q000494:pharmacology; D012235:Rhodamines; D012615:Sea Anemones / Q000502:physiology*; D012794:Sialic Acids / Q000494:pharmacology
chemical_list: D000199:Actins; D011108:Polymers; D012235:Rhodamines; D012794:Sialic Acids; D010590:Phalloidine; D011392:Proline; D003850:Deoxyribonuclease I; D019158:N-Acetylneuraminic Acid