title: The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila.
abstract: Tiggrin is a novel extracellular matrix ligand for the Drosophila PS2 integrins. We have used flanking P elements to generate a precise deletion of tiggrin. Most flies lacking tiggrin die as larvae or pupae. A few adults do emerge and these appear to be relatively normal, displaying only misshapen abdomens and a low frequency of wing defects. Examination of larvae shows that muscle connections, function and morphology are defective in tiggrin mutants. Muscle contraction waves that extend the length of the larvae are much slower in tiggrin mutants. Direct examination of bodywall muscles shows defects in muscle attachment sites, where tiggrin is specifically localized, and muscles appear thinner. Transgenes expressing tiggrin are capable of rescuing tiggrin mutant phenotypes. Transgenes expressing a mutant tiggrin, whose Arg-Gly-Asp (RGD) integrin recognition sequence has been mutated to Leu-Gly-Ala (LGA) show much reduced, but significant, rescuing ability. Cell spreading assays detect no interactions of this mutant tiggrin with PS2 integrins. Therefore, while the RGD sequence is critical for PS2 interactions and full activity in the whole fly, the mutant tiggrin retains some function(s) that are probably mediated by interactions with other ECM molecules or cell surface receptors
authors.affiliation: University of Arizona, Department of Molecular Biology, Tuscon, Arizona 85721, USA. tbunch@u.arizona.edu
authors.forename: T A
authors.initials: TA
authors.lastname: Bunch
authors.forename: M W
authors.initials: MW
authors.lastname: Graner
authors.forename: L I
authors.initials: LI
authors.lastname: Fessler
authors.forename: J H
authors.initials: JH
authors.lastname: Fessler
authors.forename: K D
authors.initials: KD
authors.lastname: Schneider
authors.forename: A
authors.initials: A
authors.lastname: Kerschen
authors.forename: L P
authors.initials: LP
authors.lastname: Choy
authors.forename: B W
authors.initials: BW
authors.lastname: Burgess
authors.forename: D L
authors.initials: DL
authors.lastname: Brower
mesh_terms: D000005:Abdomen; D000818:Animals; D030801:Animals, Genetically Modified; D004330:Drosophila / Q000196:embryology / Q000235:genetics / Q000502:physiology*; D029721:Drosophila Proteins; D016326:Extracellular Matrix Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D017344:Genes, Insect / Q000502:physiology; D005804:Genes, Lethal / Q000502:physiology; D039001:Integrin alpha Chains; D016023:Integrins; D007814:Larva; D008024:Ligands; D009119:Muscle Contraction / Q000235:genetics*; D009132:Muscles / Q000196:embryology / Q000502:physiology; D009154:Mutation; D009842:Oligopeptides / Q000494:pharmacology / Q000502:physiology; D010641:Phenotype; D011679:Pupa; D012333:RNA, Messenger / Q000235:genetics; D014921:Wings, Animal
chemical_list: D029721:Drosophila Proteins; D016326:Extracellular Matrix Proteins; D039001:Integrin alpha Chains; D016023:Integrins; D008024:Ligands; D009842:Oligopeptides; D012333:RNA, Messenger; C089678:Tig protein, Drosophila; C082188:if protein, Drosophila; C047981:arginyl-glycyl-aspartic acid