ArticleThe Journal of cell biology1994
Identification of secreted and cytosolic gelsolin in Drosophila.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Comparative proteomics of stenotopic caddisfly Crunoecia irrorata identifies acclimation strategies to warming.Molecular ecology · 2019Article
- A Cell Density-Dependent Reporter in the Drosophila S2 Cells.Scientific reports · 2019Article
- Lifestyle and host defense mechanisms of the dung beetle, Euoniticellus intermedius: the toll signaling pathway.Journal of insect science (Online) · 2013Article
- Mass spectrometric characterization of gelsolin isoforms.Rapid communications in mass spectrometry : RCM · 2010Article
- Comparative analysis of proteome maps of silkworm hemolymph during different developmental stages.Proteome science · 2010Article
- Systematic analysis of the transcriptional switch inducing migration of border cells.Developmental cell · 2006Article
- Molecular and mutational analysis of a gelsolin-family member encoded by the flightless I gene of Drosophila melanogaster.Genetics · 1995Article
- Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.The Biochemical journal · 1995Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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