Regulation of translation and proteolysis during the development of embryonic dorso-ventral polarity in Drosophila. Homology of easter proteinase with Limulus proclotting enzyme and translational activation of Toll receptor synthesis.

doi:10.1016/0167-4781(92)90163-t

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Article

Regulation of translation and proteolysis during the development of embryonic dorso-ventral polarity in Drosophila. Homology of easter proteinase with Limulus proclotting enzyme and translational activation of Toll receptor synthesis.

Biochimica et biophysica acta - 20 Oct 1992

Gay N J, Keith F J

Abstract excerpt

The generation of dorso-ventral polarity during Drosophila embryogenesis is regulated by the action of 12 maternally expressed gene products, the dorsal group. These products act together to form a dorso-ventral nuclear gradient of the transcription factor dorsal. At least three of the dorsal gro...

Topics

Amino Acid Sequence
Animals
Disulfides
Drosophila
Drosophila Proteins
Endopeptidases
Enzyme Precursors
Gene Expression Regulation
Horseshoe Crabs
Insect Hormones
Membrane Glycoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Phenotype

Protein Biosynthesis

Receptors, Cell Surface

Sequence Homology, Amino Acid

Serine Endopeptidases

Toll-Like Receptors

Source

Open in PubMed

Identifiers

PMID: 1420309
DOI: 10.1016/0167-4781(92)90163-t

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1420309-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Regulation of translation and proteolysis during the development of embryonic dorso-ventral polarity in Drosophila. Homology of easter proteinase with Limulus proclotting enzyme and translational activation of Toll receptor synthesis.PMID 1420309Read ↗

Regulation of Easter activity is required for shaping the Dorsal gradient in the Drosophila embryo.Semantic proximity Read ↗

Activation of Snake in a serine protease cascade that defines the dorsoventral axis is atypical and pipe-independent in Drosophila embryos.Semantic proximity Read ↗

Proteolytic processing of the Drosophila Spätzle protein by easter generates a dimeric NGF-like molecule with ventralising activity.Semantic proximity Read ↗

Mutational analysis of the Drosophila snake protease: an essential role for domains within the proenzyme polypeptide chain.Semantic proximity Read ↗

Multiple isoforms of the Drosophila Spätzle protein are encoded by alternatively spliced maternal mRNAs in the precellular blastoderm embryo.Semantic proximity Read ↗

Activation of the kinase Pelle by Tube in the dorsoventral signal transduction pathway of Drosophila embryo.Semantic proximity Read ↗

Three-dimensional models of proteases involved in patterning of the Drosophila Embryo. Crucial role of predicted cation binding sites.Semantic proximity Read ↗

Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo.Semantic proximity Read ↗

The Toll pathway is required in the epidermis for muscle development in the Drosophila embryo.Semantic proximity Read ↗

Dominant and recessive alleles of the Drosophila easter gene are point mutations at conserved sites in the serine protease catalytic domain.Semantic proximity Read ↗

Ventralization of the Drosophila embryo by deletion of extracellular leucine-rich repeats in the Toll protein.Semantic proximity Read ↗

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