ArticleMolecular and cellular biology1998
Functional dissection of YA, an essential, developmentally regulated nuclear lamina protein in Drosophila melanogaster.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 14 citations in OpenAlex.
- The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains.Molecular biology of the cell · 2002Article
- Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA.Molecular and cellular biology · 1998Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The Drosophila YA protein is a nuclear lamina component whose function is essential to initiate embryonic development. To identify regions of YA required for its action in its normal cellular context, we made targeted mutations in the YA protein and tested their consequences in flies and embryos in vivo. We found that critical amino acids are distributed along the length of the YA molecule, with functionally important regions including the N- and the C-terminal ends, the cysteine residues in YA's two potential zinc fingers, a serine/threonine-rich region, and a potential maturation-promoting factor or mitogen-activated protein kinase phosphorylation target site, ITPIR. In addition, several Ya mutations showed intragenic complementation, with N-terminal mutations complementing C-terminal mutations, suggesting that YA proteins interact with one another. In support of this interaction, we demonstrated by immunoprecipitation that YA molecules are present in complexes with each other. Finally, we showed that the C-terminal 179 amino acids of YA are necessary to target, or retain, YA in the nuclear envelope.
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