The Arf-GEF Steppke promotes F-actin accumulation, cell protrusions and tissue sealing during Drosophila dorsal closure

Autor: Tony J. C. Harris, Junior J. West
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Embryology
Heredity
Mutant
Cell Membranes
Cell
Regulator
Biochemistry
Contractile Proteins
0302 clinical medicine
Myosin
Medicine and Health Sciences
Drosophila Proteins
Guanine Nucleotide Exchange Factors
Skin
0303 health sciences
Heterozygosity
Multidisciplinary
biology
Chemistry
Drosophila Melanogaster
030302 biochemistry & molecular biology
Eukaryota
Animal Models
Actomyosin
Cell biology
Insects
Pleckstrin homology domain
Intercellular Junctions
medicine.anatomical_structure
Experimental Organism Systems
Cell Processes
Medicine
Drosophila
Anatomy
Integumentary System
Cellular Structures and Organelles
Drosophila melanogaster
Research Article
Leading edge
Arthropoda
Science
Motor Proteins
Actin Motors
Embryonic Development
macromolecular substances
Myosins
Research and Analysis Methods
03 medical and health sciences
Model Organisms
Protein Domains
Molecular Motors
Genetics
medicine
Animals
Actin
030304 developmental biology
Embryos
Organisms
Biology and Life Sciences
Proteins
Membrane Proteins
Cell Biology
biology.organism_classification
Invertebrates
Actins
Dorsal closure
Cytoskeletal Proteins
Membrane protein
Animal Studies
Cell Surface Extensions
Epidermis
Zoology
Entomology
030217 neurology & neurosurgery
Developmental Biology
Actin Polymerization
Zdroj: PLoS ONE, Vol 15, Iss 11, p e0239357 (2020)
PLoS ONE
ISSN: 1932-6203
Popis: Cytohesin Arf-GEFs promote actin polymerization and protrusions of cultured cells, whereas the Drosophila cytohesin, Steppke, antagonizes actomyosin networks in several developmental contexts. To reconcile these findings, we analyzed epidermal leading edge actin networks during Drosophila embryo dorsal closure. Here, Steppke is required for F-actin of the actomyosin cable and for actin-based protrusions. steppke mutant defects in the leading edge actin networks are associated with improper sealing of the dorsal midline, but are distinguishable from effects of myosin mis-regulation. Steppke localizes to leading edge cell-cell junctions with accumulations of the F-actin regulator Enabled emanating from either side. Enabled requires Steppke for full leading edge recruitment, and genetic interaction shows the proteins cooperate for dorsal closure. Inversely, Steppke over-expression induces ectopic, actin-rich, lamellar cell protrusions, an effect dependent on the Arf-GEF activity and PH domain of Steppke, but independent of Steppke recruitment to myosin-rich AJs via its coiled-coil domain. Thus, Steppke promotes actin polymerization and cell protrusions, effects that occur in conjunction with Steppke’s previously reported regulation of myosin contractility during dorsal closure.
Databáze: OpenAIRE
Externí odkaz:
Nepřihlášeným uživatelům se plný text nezobrazuje