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Drosophila ELMO/CED-12 interacts with Myoblast city to direct myoblast fusion and ommatidial organization.
- Source :
-
Developmental biology [Dev Biol] 2008 Feb 01; Vol. 314 (1), pp. 137-49. Date of Electronic Publication: 2007 Nov 28. - Publication Year :
- 2008
-
Abstract
- Members of the CDM (CED-5, Dock180, Myoblast city) superfamily of guanine nucleotide exchange factors function in diverse processes that include cell migration and myoblast fusion. Previous studies have shown that the SH3, DHR1 and DHR2 domains of Myoblast city (MBC) are essential for it to direct myoblast fusion in the Drosophila embryo, while the conserved DCrk-binding proline rich region is expendable. Herein, we describe the isolation of Drosophila ELMO/CED-12, an approximately 82 kDa protein with a pleckstrin homology (PH) and proline-rich domain, by interaction with the MBC SH3 domain. Mass spectrometry confirms the presence of an MBC/ELMO complex within the embryonic musculature at the time of myoblast fusion and embryos maternally and/or zygotically mutant for elmo exhibit defects in myoblast fusion. Overexpression of MBC and ELMO in the embryonic mesoderm causes defects in myoblast fusion reminiscent of those seen with constitutively-activated Rac1, supporting the previous finding that both the absence of and an excess of Rac activity are deleterious to myoblast fusion. Overexpression of MBC and ELMO/CED-12 in the eye causes perturbations in ommatidial organization that are suppressed by mutations in Rac1 and Rac2, demonstrating genetically that MBC and ELMO/CED-12 cooperate to activate these small GTPases in Drosophila.
- Subjects :
- Animals
Blood Proteins metabolism
Cell Fusion
Compound Eye, Arthropod embryology
Drosophila melanogaster embryology
Mesoderm embryology
Mesoderm physiology
Muscles embryology
Muscles physiology
Phosphoproteins metabolism
Protein Binding
rac GTP-Binding Proteins metabolism
rac1 GTP-Binding Protein metabolism
src Homology Domains
RAC2 GTP-Binding Protein
Adaptor Proteins, Signal Transducing metabolism
Cell Movement physiology
Cytoskeletal Proteins metabolism
Drosophila Proteins metabolism
Drosophila melanogaster physiology
Myoblasts physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1095-564X
- Volume :
- 314
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Developmental biology
- Publication Type :
- Academic Journal
- Accession number :
- 18163987
- Full Text :
- https://doi.org/10.1016/j.ydbio.2007.11.022