Copy the page URI to the clipboard
Zhu, Min-Yan
(1999).
DOI: https://doi.org/10.21954/ou.ro.0000ff60
Abstract
Gelsolin is an actin-binding protein that under the control of calcium ions and polyphosphoinositide can either sever and cap the actin filaments therefore breakdown the actin networks, or initiate the formation of actin filaments and the actin networks. Studies of gelsolin in mammals have shown that gelsolin is the substrate of various signal cascades and on the other hand it can modulate lipid signaling.
The function of gelsolin during Drosophila development is unclear due to the lack of gelsolin mutants. A previous attempt to generate a gelsolin mutant in an extensive EMS screen failed, which implies that either gelsolin is not easily chemically mutable or loss of gelsolin function is not lethal. A different approach, P-element mediated mutagenesis is employed in the work presented here to generate a gelsolin null mutant. A PCR based screen was developed to identify gelsolin mutants without prior knowledge of their phenotype.
However the screen was not successful despite the fact that the screen was large and sensitive. No gelsolin mutants were found, suggesting that the gelsolin locus can also not be easily mutated by P-element mediated mutagenesis.