Identification of secreted and cytosolic gelsolin in Drosophila.
Open Access
- 1 May 1994
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 125 (3) , 607-616
- https://doi.org/10.1083/jcb.125.3.607
Abstract
We have cloned the gene for Drosophila gelsolin. Two mRNAs are produced from this gene by differential splicing. The protein encoded by the longer mRNA has a signal peptide and its electrophoretic mobility when translated in vitro in the presence of microsomes is higher than when it is translated without microsomes. The protein translated from the shorter mRNA does not show this difference. This indicates that Drosophila like vertebrates has two forms of gelsolin, one secreted, the other cytoplasmic. The mRNA for both is present ubiquitously in the early embryo. Later, the cytoplasmic form is expressed in parts of the gut. The RNA for the secreted form is expressed in the fat body, and the secreted protein is abundant in extracellular fluid (hemolymph). The cytoplasmic form of gelsolin co-localizes with F-actin in the cortex of the cells in the embryo and in larval epithelia. However, during cellularization of the blastoderm it is reduced at the base of the cleavage furrow, a structure similar to the contractile ring in dividing cells.Keywords
This publication has 47 references indexed in Scilit:
- Cloning of a Secretory Gelsolin from Drosophila melanogasterJournal of Molecular Biology, 1993
- The signal peptideThe Journal of Membrane Biology, 1990
- Calcium and polyphosphoinositide control of cytoskeletal dynamicsTrends in Neurosciences, 1989
- Actin-binding proteins from Drosophila embryos: a complex network of interacting proteins detected by F-actin affinity chromatography.The Journal of cell biology, 1989
- Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.The Journal of cell biology, 1988
- Nucleotide sequence of pig plasma gelsolin: Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeatsJournal of Molecular Biology, 1988
- Functional cDNA libraries from Drosophila embryosJournal of Molecular Biology, 1988
- A re-evaluation of cytoplasmic gelsolin localization.The Journal of cell biology, 1986
- A 45,000-mol-wt protein from unfertilized sea urchin eggs severs actin filaments in a calcium-dependent manner and increases the steady-state concentration of nonfilamentous actin.The Journal of cell biology, 1984
- F-actin distribution during the cellularization of the embryo visualized with FL-phalloidinExperimental Cell Research, 1983