title: A Common Suite of Coagulation Proteins Function in Drosophila Muscle Attachment.
abstract: The organization and stability of higher order structures that form in the extracellular matrix (ECM) to mediate the attachment of muscles are poorly understood. We have made the surprising discovery that a subset of clotting factor proteins are also essential for muscle attachment in the model organism Drosophila melanogaster One such coagulation protein, Fondue (Fon), was identified as a novel muscle mutant in a pupal lethal genetic screen. Fon accumulates at muscle attachment sites and removal of this protein results in decreased locomotor behavior and detached larval muscles. A sensitized genetic background assay reveals that fon functions with the known muscle attachment genes Thrombospondin (Tsp) and Tiggrin (Tig). Interestingly, Tig is also a component of the hemolymph clot. We further demonstrate that an additional clotting protein, Larval serum protein 1γ (Lsp1γ), is also required for muscle attachment stability and accumulates where muscles attach to tendons. While the local biomechanical and organizational properties of the ECM vary greatly depending on the tissue microenvironment, we propose that shared extracellular protein-protein interactions influence the strength and elasticity of ECM proteins in both coagulation and muscle attachment.
authors: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas 66506.
authors: Nicole
authors: N
authors: Green
authors: Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, Missouri 64110.
authors: Nadia
authors: N
authors: Odell
authors: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas 66506.
authors: Molly
authors: M
authors: Zych
authors: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas 66506.
authors: Cheryl
authors: C
authors: Clark
authors: Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, Missouri 64110.
authors: Zong-Heng
authors: ZH
authors: Wang
authors: Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, Missouri 64110.
authors: Bridget
authors: B
authors: Biersmith
authors: Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616.
authors: Clara
authors: C
authors: Bajzek
authors: Department of Biology, Indiana University, Bloomington, Indiana 47405.
authors: Kevin R
authors: KR
authors: Cook
authors: Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616.|Department of Entomology, Cornell University, Ithaca, New York 14853.
authors: Mitchell S
authors: MS
authors: Dushay
authors: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas 66506 geisbrechte@ksu.edu.|Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, Missouri 64110.
authors: Erika R
authors: ER
authors: Geisbrecht
mesh_terms: D000818:Animals; D001779:Blood Coagulation Factors / Q000235:genetics / Q000378:metabolism*; D001798:Blood Proteins / Q000235:genetics / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000235:genetics* / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism; D006458:Hemolymph / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000502:physiology; D011485:Protein Binding; D013710:Tendons / Q000378:metabolism* / Q000502:physiology; D019699:Thrombospondins / Q000235:genetics / Q000378:metabolism
chemical_list: D001779:Blood Coagulation Factors; D001798:Blood Proteins; D029721:Drosophila Proteins; D016326:Extracellular Matrix Proteins; D019699:Thrombospondins; C089678:Tig protein, Drosophila; C512855:fon protein, Drosophila; C034648:larval serum protein, Drosophila
keywords: Drosophila; Fondue; Tiggrin; muscle attachment sites